SWISS-MODEL Homology Modelling Report

Model Building Report

This document lists the results for the homology modelling project "Q838A4-MurE-E-faecalis" submitted to SWISS-MODEL workspace on Oct. 17, 2017, 6:22 p.m..The submitted primary amino acid sequence is given in Table T1.

If you use any results in your research, please cite the relevant publications:

Marco Biasini; Stefan Bienert; Andrew Waterhouse; Konstantin Arnold; Gabriel Studer; Tobias Schmidt; Florian Kiefer; Tiziano Gallo Cassarino; Martino Bertoni; Lorenza Bordoli; Torsten Schwede. (2014). SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Research (1 July 2014) 42 (W1): W252-W258; doi: 10.1093/nar/gku340.
Arnold, K., Bordoli, L., Kopp, J. and Schwede, T. (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics, 22, 195-201.
Benkert, P., Biasini, M. and Schwede, T. (2011) Toward the estimation of the absolute quality of individual protein structure models. Bioinformatics, 27, 343-350

Results

The SWISS-MODEL template library (SMTL version 2017-10-11, PDB release 2017-10-06) was searched with Blast (Altschul et al., 1997) and HHBlits (Remmert, et al., 2011) for evolutionary related structures matching the target sequence in Table T1. For details on the template search, see Materials and Methods. Overall 384 templates were found (Table T2).

Models

The following models were built (see Materials and Methods "Model Building"):

Model #01

FileBuilt withOligo-StateLigandsGMQEQMEAN
PDB ProMod3 Version 1.0.2. MONOMER
1 x MG: MAGNESIUM ION;
0.64-4.54
QMEAN-4.54
-2.58
All Atom-2.27
Solvation-1.02
Torsion-3.81
TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityRangeCoverageDescription
2wtz.1.A30.17monomerHHblitsX-ray3.00Å0.35 1 - 506 0.93UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE
LigandAdded to ModelDescription
MG
MAGNESIUM ION
UAG✕ - Binding site not conserved.
URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE-D-GLUTAMATE

Target    MTISLFAIRDCLE----KEDLLKEFISPEGWHLTLSDTLGQREVTALSYDSRDVTAETLFFC-KGLNFK-EIYLENAVKD
2wtz.1.A VGVRLAALADQVGAALAEG-PAQRA-V-------TE----DRTVTGVTLRAQDVSPGDLFAALTGSTTHGARHVGDAIAR

Target GLEIYVSEVPY-EV----PAQLGIIVTDIKKAMAVLSMAFYDYPQNKLKLIGFTGTKGKTTAAYFTKYILDVATQQKTAL
2wtz.1.A GAVAVLTDPAGVAEIAGRAAVPVLVHPAPRGVLGGLAATVYGHPSERLTVIGITGTSGKTTTTYLVEAGLRA-AGRVAGL

Target LSTMNSTLDGKTFFKSALTTPESLDLYRMMATAVANGMTHFIMEVSSQAYKTNRVYKLFFDVGIFLNITPDHISPIEHPT
2wtz.1.A IGTIGIRVGGADL-PSALTTPEAPTLQAMLAAMVERGVDTVVMEVSSHALALGRVDGTRFAVGAFTNLSRDHLD--FHPS

Target FDDYFYCKRQLITHS-----KVIVLNHEADYFPLLKETAQQQKVPAIVYGS-QPAPEVDYSFAV---SSEDSLRFIVESP
2wtz.1.A MADYFEAKASLFDPDSALRARTAVVCIDDDAGRAMAARA----ADAITVSAADR--PAHWRATDVAPTDAGGQQFTAIDP

Target ADALGLAG-SYHLRLGGDFNKGNALSAAIASVLVGASKEECQQGIAATT-VPGRMESLTNTNGATVYVDYAHNYDSLKNL
2wtz.1.A AG----VGHHIGIRLPGRYNVANCLVALAILDTVGVSPEQAVPGLRE-IRVPGRLEQIDRGQGFLALVDYAHKPEALRSV

Target LTFVREEHPDGRLIVLVGSTGDKAISRRKDFGRVLSELADVAVLTTDDPASEDPAKICQEIQAHITKEM---PVYTVLDR
2wtz.1.A LTTLAH--PDRRLAVVFGAGGDRDPGKRAPMGRIAAQLADLVVVTDDNPRDEDPTAIRREILAGAAEVGGDAQVVEIADR

Target GEAIAHALSLSTTADDAIVLAGKGADLYQKVNGVDEPYAGDFALAEAFINKKN
2wtz.1.A RDAIRHAVAW-ARPGDVVLIAGKGHETGQRGGGRVRPF-DDRVELAAALEA--




Model #02

FileBuilt withOligo-StateLigandsGMQEQMEAN
PDB ProMod3 Version 1.0.2. MONOMER
1 x MG: MAGNESIUM ION;
0.63-3.68
QMEAN-3.68
-2.13
All Atom-1.33
Solvation-0.50
Torsion-3.22
TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityRangeCoverageDescription
4bub.2.A32.00monomerHHblitsX-ray2.90Å0.35 37 - 507 0.89UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--LD-LYSINE LIGASE
LigandAdded to ModelDescription
MG
MAGNESIUM ION
ADP✕ - Binding site not conserved.
ADENOSINE-5'-DIPHOSPHATE

Target    MTISLFAIRDCLEKEDLLKEFISPEGWHLTLSDTLGQREVTALSYDSRDVTAETLFFC-KGLNFK-EIYLENAVKDGLEI
4bub.2.A ------------------------------------DLEITGVSNHSSKVKKGDLFICRRGEKFDSHEIIPEVMEKGAVA

Target YVSEVPYEVPAQLGIIVTDIKKAMAVLSMAFYDYPQNKLKLIGFTGTKGKTTAAYFTKYILDVATQQKTALLSTMNSTLD
4bub.2.A VVVEREID-LDFPYIQVFDSRYFEAKVASLFFEDPWKDVLTFGVTGTNGKTTTTMMIYHMLTS-LGERGSVLTTAVKRIL

Target GKTFFKSALTTPESLDLYRMMATAVANGMTHFIMEVSSQAYKTNRVYKLFFDVGIFLNITPDHISPIEHPTFDDYFYCKR
4bub.2.A GNSY-YDDITTPDAITILSAMKENREGGGKFFALEVSSHALVQQRVEGVRFDVGIFTNISRDHLD--FHGTFENYLKAKL

Target QLITH---SKVIVLNHEADYFPLLKETAQQQKVPAIVYGSQPAPEVDYSFAV--SSEDSLRFIVESPADALGLAGSYHLR
4bub.2.A HLFDLLKDDGVAVLNES--LADAFNR--K---SRKITFGTSK--NADYRLGNIEVSWEGTQFVLETPDG----LLKVFTR

Target LGGDFNKGNALSAAIASVLVGASKEECQQGIAATT-VPGRMESLTN--TNGATVYVDYAHNYDSLKNLLTFVREEHPDGR
4bub.2.A AIGDFNAYNAAAAIAALHQLGYDPKDLASSLETFTGVEGRFEVVRGAKKIGLNVVVDFAHSPDALEKLLKNVR-KISQGR

Target LIVLVGSTGDKAISRRKDFGRVLSELADVAVLTTDDPASEDPAKICQEIQAHITKEMPVYTVLDRGEAIAHALSLSTTAD
4bub.2.A VIVVFGAGGNSDRGKRPMMSEVASKLADVVILTTDDPRGEDPEQIMEDLIKGIDKRKPYLVLFDRREAIETALTI-ANRG

Target DAIVLAGKGADLYQKVNG-VDEPYAGDFALAEAFINKKN
4bub.2.A DSVVIAGRGHERYQIIDEEKKVPF-QDREVVEEIIRDK-




Model #03

FileBuilt withOligo-StateLigandsGMQEQMEAN
PDB ProMod3 Version 1.0.2. MONOMER
None
0.52-6.84
QMEAN-6.84
-4.98
All Atom-3.53
Solvation-2.20
Torsion-5.42
TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityRangeCoverageDescription
2am2.1.A18.08monomerHHblitsX-ray2.80Å0.30 1 - 486 0.84UDP-N-acetylmuramoylalanine-D-glutamyl-lysine-D-alanyl-D-alanine ligase, MurF protein
LigandAdded to ModelDescription
2LG✕ - Binding site not conserved.
2-CHLORO-N-(3-CYANO-5,6-DIHYDRO-4H-CYCLOPENTA[B]THIOPHEN-2-YL)-5-DIETHYLSULFAMOYL-BENZAMIDE

Target    MTISLFAIRDCLEKEDLLKEFISPEGWHLTLSDTLGQREVTALSYDSRDVTAETLFFC-KGLNFK-EIYLENAVKDGLEI
2am2.1.A MKLTIHEIAQVVGAKNDI-S--I-------FE----DTQLEKAEFDSRLIGTGDLFVPLKGA-RDGHDFIETAFENGAAV

Target YVSEVPYEVPAQLGIIVTDIKKAMAVLSMAFYDYPQNKLKLIGFTGTKGKTTAAYFTKYILDVATQQKTALLSTMNSTLD
2am2.1.A TLSEKEVS--NHPYILVDDVLTAFQSLASYYLEKT--TVDVFAVTGSNGKTTTKDMLAHLLST-RYKT---YKTQGNY--

Target GKTFFKSALTTPESLDLYRMMATAVANGMTHFIMEVSSQA-YKTN-RVYKLFFDVGIFLNITPDHISPIEHPTFDDYFYC
2am2.1.A -----NNEIGLPYT--VLH-----MPEGTEKLVLEMGQDHLGDIHLLSELARPKTAIVTLVGEAHLA--FFKDRSEIAKG

Target KRQLIT---HSKVIVLNHEADYFPLLKETAQQQKVPAIVYGSQPAPEVDY-SFAVSSEDSLRFIVESPADALGLAGSYHL
2am2.1.A KMQIADGMASGSLLLAPADPIVE-DYLP-I---DKKVVRFGQGA--ELEITDLVERK-DSLTFKANFL-E----Q-ALDL

Target RLGGDFNKGNALSAAIASVLVGASKEECQQGIAATT-VPGRMESLTNTNGATVYVD-YAHNYDSLKNLLTFVREEH--PD
2am2.1.A PVTGKYNATNAMIASYVALQEGVSEEQIRLAFQHLELTRNRTEWKKAANGADILSDVYNANPTAMKLILETFSAIPANEG

Target GRLIVLVGST---GDKAISRRKDFGRVLSEL-ADVAVLTTDDPASEDPAKICQEIQAHITKEMPVYTVLD------RGEA
2am2.1.A GKKIAVLADMKELGDQSVQLHNQMILSLSPDVLDIVIFYGED-----IAQLAQLASQMFP-IGHVYYFKKTEDQDQFEDL

Target IAHALSLSTTADDAIVLAGKGADLYQKVNGVDEPYAGDFALAEAFINKKN
2am2.1.A VKQVKES-LGAHDQILLKGSNSMNLAKL----------------------




Model #04

FileBuilt withOligo-StateLigandsGMQEQMEAN
PDB ProMod3 Version 1.0.2. MONOMER
None
0.43-8.38
QMEAN-8.38
-4.72
All Atom-4.24
Solvation-3.08
Torsion-7.05
TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityRangeCoverageDescription
1eeh.1.A17.41monomerHHblitsX-ray1.90Å0.29 43 - 484 0.75UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
LigandAdded to ModelDescription
UMA✕ - Binding site not conserved.
URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE

Target    MTISLFAIRDCLEKEDLLKEFISPEGWHLTLSDTLGQREVTALSYDSRDVTAETLFFCKGLNF--K-EIYLENAVKDGLE
1eeh.1.A ------------------------------------------RVMDTRMTPPGLDKLPEAVERHTGSLN--DE-WLMAAD

Target IYVSEVPYEVPAQLGIIVTD--IKKAMAVLSMAFYDYPQNKLKLIGFTGTKGKTTAAYFTKYILDVATQQKTALLSTMNS
1eeh.1.A LIVASPGIA-LAHPSLSAAADAGIEIVGDIELFCR---EAQAPIVAITGSNGKSTVTTLVGEMAKA-AGVNVGVGGN---

Target TLDGKTFFKSALTTPESLDLYRMMATAVANGMTHFIMEVSSQAYKTNRVYKLFFDVGIFLNITPDHISPIEHP-TFDDYF
1eeh.1.A -----------IGLPAL-M-------LLDDECELYVLELSSFQ--LETTSSLQAVAATILNVTEDHMD--RYPFGLQQYR

Target YCKRQLITHSKVIVLNHEADYFPLLKETAQQQKVPAIVYGSQPAPEVDYSFAVSSEDSLRFIVESPADALGLAGSYHLRL
1eeh.1.A AAKLRIYENAKVCVVNADDALTMPIRG----ADERCVSFGVNM---GDYHLNHQQGETW-LRV--KGEK--VLNVKEMKL

Target GGDFNKGNALSAAIASVLVGASKEECQQGIAATT-VPGRMESLTNTNGATVYVDY-AHNYDSLKNLLTFVREEHPDGRLI
1eeh.1.A SGQHNYTNALAALALADAAGLPRASSLKALTTFTGLPHRFEVVLEHNGVRWINDSKATNVGSTEAALNGLH--V-DGTLH

Target VLVGSTGDKAISRRKDFGRVLSELADVAVLTTDDPASEDPAKICQEIQAHITKEMPVYTVLDRGEAIAHALSLSTTADDA
1eeh.1.A LLLGGDG-KSAD-FSPLARYLNGDNVRLYCFGRD-----GAQLAALRPE------VAEQTETMEQAMRLLAPR-VQPGDM

Target IVLAGKGADLYQKVNGVDEPYAGDFALAEAFINKKN
1eeh.1.A VLLSPACASLDQ------------------------




Materials and Methods

Template Search

Template search with Blast and HHBlits has been performed against the SWISS-MODEL template library (SMTL, last update: 2017-10-11, last included PDB release: 2017-10-06).

The target sequence was searched with BLAST (Altschul et al., 1997) against the primary amino acid sequence contained in the SMTL. A total of 6 templates were found.

An initial HHblits profile has been built using the procedure outlined in (Remmert, et al., 2011), followed by 1 iteration of HHblits against NR20. The obtained profile has then be searched against all profiles of the SMTL. A total of 380 templates were found.

Template Selection

For each identified template, the template's quality has been predicted from features of the target-template alignment. The templates with the highest quality have then been selected for model building.

Model Building

Models are built based on the target-template alignment using ProMod3. Coordinates which are conserved between the target and the template are copied from the template to the model. Insertions and deletions are remodelled using a fragment library. Side chains are then rebuilt. Finally, the geometry of the resulting model is regularized by using a force field. In case loop modelling with ProMod3 fails, an alternative model is built with PROMOD-II (Guex, et al., 1997).

Model Quality Estimation

The global and per-residue model quality has been assessed using the QMEAN scoring function (Benkert, et al., 2011) . For improved performance, weights of the individual QMEAN terms have been trained specifically for SWISS-MODEL.

Ligand Modelling

Ligands present in the template structure are transferred by homology to the model when the following criteria are met (Gallo -Casserino, to be published): (a) The ligands are annotated as biologically relevant in the template library, (b) the ligand is in contact with the model, (c) the ligand is not clashing with the protein, (d) the residues in contact with the ligand are conserved between the target and the template. If any of these four criteria is not satisfied, a certain ligand will not be included in the model. The model summary includes information on why and which ligand has not been included.

Oligomeric State Conservation

Homo-oligomeric structure of the target protein is predicted based on the analysis of pairwise interfaces of the identified template structures. For each relevant interface between polypeptide chains (interfaces with more than 10 residue-residue interactions), the QscoreOligomer (Mariani et al., 2011) is predicted from features such as similarity to target and frequency of observing this interface in the identified templates (Kiefer, Bertoni, Biasini, to be published). The prediction is performed with a random forest regressor using these features as input parameters to predict the probability of conservation for each interface. The QscoreOligomer of the whole complex is then calculated as the weight-averaged QscoreOligomer of the interfaces. The oligomeric state of the target is predicted to be the same as in the template when QscoreOligomer is predicted to be higher or equal to 0.5.

References

Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W. and Lipman, D.J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res, 25, 3389-3402.
Remmert, M., Biegert, A., Hauser, A. and Soding, J. (2012) HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment. Nat Methods, 9, 173-175.
Guex, N. and Peitsch, M.C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis, 18, 2714-2723.
Sali, A. and Blundell, T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol, 234, 779-815.
Benkert, P., Biasini, M. and Schwede, T. (2011) Toward the estimation of the absolute quality of individual protein structure models. Bioinformatics, 27, 343-350.
Mariani, V., Kiefer, F., Schmidt, T., Haas, J. and Schwede, T. (2011) Assessment of template based protein structure predictions in CASP9. Proteins, 79 Suppl 10, 37-58.

Table T1:

Primary amino acid sequence for which templates were searched and models were built.

MTISLFAIRDCLEKEDLLKEFISPEGWHLTLSDTLGQREVTALSYDSRDVTAETLFFCKGLNFKEIYLENAVKDGLEIYVSEVPYEVPAQLGIIVTDIKK
AMAVLSMAFYDYPQNKLKLIGFTGTKGKTTAAYFTKYILDVATQQKTALLSTMNSTLDGKTFFKSALTTPESLDLYRMMATAVANGMTHFIMEVSSQAYK
TNRVYKLFFDVGIFLNITPDHISPIEHPTFDDYFYCKRQLITHSKVIVLNHEADYFPLLKETAQQQKVPAIVYGSQPAPEVDYSFAVSSEDSLRFIVESP
ADALGLAGSYHLRLGGDFNKGNALSAAIASVLVGASKEECQQGIAATTVPGRMESLTNTNGATVYVDYAHNYDSLKNLLTFVREEHPDGRLIVLVGSTGD
KAISRRKDFGRVLSELADVAVLTTDDPASEDPAKICQEIQAHITKEMPVYTVLDRGEAIAHALSLSTTADDAIVLAGKGADLYQKVNGVDEPYAGDFALA
EAFINKKN

Table T2:

TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityCoverageDescription
2xja.1.A30.17monomerHHblitsX-ray3.00Å0.350.93UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE
2wtz.1.A30.17monomerHHblitsX-ray3.00Å0.350.93UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE
4bub.1.A32.00monomerHHblitsX-ray2.90Å0.350.89UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--LD-LYSINE LIGASE
4bub.2.A32.00monomerHHblitsX-ray2.90Å0.350.89UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--LD-LYSINE LIGASE
4c12.1.A28.95homo-dimerBLASTX-ray1.80Å0.350.88UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--L-LYSINE LIGASE
4c12.1.A28.19homo-dimerHHblitsX-ray1.80Å0.340.89UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--L-LYSINE LIGASE
2xja.1.A31.97monomerBLASTX-ray3.00Å0.360.87UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE
2wtz.1.A31.97monomerBLASTX-ray3.00Å0.360.87UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE
1e8c.1.A26.54monomerHHblitsX-ray2.00Å0.330.90UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE
4bub.1.A34.11monomerBLASTX-ray2.90Å0.370.84UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--LD-LYSINE LIGASE
4bub.2.A34.11monomerBLASTX-ray2.90Å0.370.84UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--LD-LYSINE LIGASE
1e8c.1.A31.24monomerBLASTX-ray2.00Å0.350.84UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE
2am2.1.A18.08monomerHHblitsX-ray2.80Å0.300.84UDP-N-acetylmuramoylalanine-D-glutamyl-lysine-D-alanyl-D-alanine ligase, MurF protein
3zm5.1.A18.20monomerHHblitsX-ray2.94Å0.300.83UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE
4cvl.1.A21.04monomerHHblitsX-ray2.98Å0.300.83UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE
4cvm.1.A21.04monomerHHblitsX-ray2.06Å0.300.83UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D- ALANINE LIGASE
4ziy.1.A19.71monomerHHblitsX-ray1.85Å0.300.83UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
4qf5.1.A19.62monomerHHblitsX-ray2.80Å0.300.82UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
4qdi.1.A19.62monomerHHblitsX-ray1.80Å0.300.82UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
1gg4.1.A18.85monomerHHblitsX-ray2.30Å0.300.82UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMYL-2,6-DIAMINOPIMELATE-D-ALANYL-D-ALANYL LIGASE
3zl8.1.A17.13monomerHHblitsX-ray1.65Å0.290.78UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE
3lk7.1.A18.32monomerHHblitsX-ray1.50Å0.300.75UDP-N-acetylmuramoylalanine--D-glutamate ligase
2xpc.1.A17.41monomerHHblitsX-ray1.49Å0.290.75UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
1uag.1.A17.41monomerHHblitsX-ray1.95Å0.290.75UDP-N-ACETYLMURAMOYL-L-ALANINE/:D-GLUTAMATE LIGASE
1eeh.1.A17.41monomerHHblitsX-ray1.90Å0.290.75UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
2uag.1.A17.41monomerHHblitsX-ray1.70Å0.290.75PROTEIN (UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE)
1e0d.1.A17.41monomerHHblitsX-ray2.40Å0.290.75UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
5a5e.1.A17.41monomerHHblitsX-ray1.84Å0.290.75UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
5a5f.1.A17.20monomerHHblitsX-ray1.90Å0.290.74UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
2y67.1.A17.02monomerHHblitsX-ray1.85Å0.280.74UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
4buc.1.A18.63monomerHHblitsX-ray2.17Å0.290.72UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
4buc.2.A18.63monomerHHblitsX-ray2.17Å0.290.72UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
2vor.1.A19.39monomerHHblitsX-ray2.30Å0.300.71FOLYLPOLYGLUTAMATE SYNTHASE PROTEIN FOLC
2gcb.1.A19.03monomerHHblitsX-ray2.30Å0.290.69Folylpolyglutamate synthase
2gc6.1.A18.75monomerHHblitsX-ray1.90Å0.290.69Folylpolyglutamate synthase
2gca.1.A18.75monomerHHblitsX-ray2.40Å0.290.69Folylpolyglutamate synthase
1fgs.1.A19.09monomerHHblitsX-ray2.40Å0.290.69FOLYLPOLYGLUTAMATE SYNTHETASE
1jbw.1.A19.09monomerHHblitsX-ray1.85Å0.290.69FOLYLPOLYGLUTAMATE SYNTHASE
1jbv.1.A19.09monomerHHblitsX-ray1.95Å0.290.69FOLYLPOLYGLUTAMATE SYNTHASE
1w7k.1.A18.52monomerHHblitsX-ray2.10Å0.290.69FOLC BIFUNCTIONAL PROTEIN
1w78.1.A18.52monomerHHblitsX-ray1.82Å0.290.69FOLC BIFUNCTIONAL PROTEIN
2gc5.1.A18.80monomerHHblitsX-ray1.85Å0.290.69Folylpolyglutamate synthase
1o5z.1.A18.47monomerHHblitsX-ray2.10Å0.290.69folylpolyglutamate synthase/dihydrofolate synthase
3nrs.1.A17.38monomerHHblitsX-ray1.80Å0.290.69Dihydrofolate:folylpolyglutamate synthetase
3pyz.1.A17.38monomerHHblitsX-ray2.10Å0.290.69Bifunctional folylpolyglutamate synthase/dihydrofolate synthase
3hn7.1.A18.73monomerHHblitsX-ray1.65Å0.290.68UDP-N-acetylmuramate-L-alanine ligase
4hv4.1.A20.12monomerHHblitsX-ray2.25Å0.290.65UDP-N-acetylmuramate--L-alanine ligase
4hv4.2.A20.12monomerHHblitsX-ray2.25Å0.290.65UDP-N-acetylmuramate--L-alanine ligase
1p3d.1.A18.65monomerHHblitsX-ray1.70Å0.290.64UDP-N-acetylmuramate--alanine ligase
1gqq.1.A18.65homo-dimerHHblitsX-ray3.10Å0.290.64UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE
1gqq.1.B18.65homo-dimerHHblitsX-ray3.10Å0.290.64UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE
1p31.1.A18.65monomerHHblitsX-ray1.85Å0.290.64UDP-N-acetylmuramate--alanine ligase
1gqy.1.B18.65homo-dimerHHblitsX-ray1.80Å0.290.64UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE
1gqy.1.A18.65homo-dimerHHblitsX-ray1.80Å0.290.64UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE
2f00.1.A18.65homo-dimerHHblitsX-ray2.50Å0.290.64UDP-N-acetylmuramate--L-alanine ligase
1j6u.1.A18.93monomerHHblitsX-ray2.30Å0.290.62UDP-N-acetylmuramate-alanine ligase MurC
3eag.1.A17.60homo-dimerHHblitsX-ray2.55Å0.280.49UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase
3eag.1.B17.60homo-dimerHHblitsX-ray2.55Å0.280.49UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase
5vvw.1.A17.41homo-tetramerHHblitsX-ray2.30Å0.280.40UDP-N-acetylmuramate--L-alanine ligase
3mvn.1.A17.89monomerHHblitsX-ray1.90Å0.310.24UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-medo-diaminopimelate ligase
2obn.1.A10.08homo-dimerHHblitsX-ray2.30Å0.250.23Hypothetical protein
2obn.1.B10.08homo-dimerHHblitsX-ray2.30Å0.250.23Hypothetical protein
3md0.1.A18.99homo-dimerHHblitsX-ray2.45Å0.280.16Arginine/ornithine transport system ATPase
3cio.1.A17.65homo-dimerHHblitsX-ray2.50Å0.320.10Tyrosine-protein kinase etk
3cio.1.B17.65homo-dimerHHblitsX-ray2.50Å0.320.10Tyrosine-protein kinase etk
1rz3.1.A16.98monomerHHblitsX-ray1.90Å0.270.10hypothetical protein RBSTP0775
4c0b.1.A9.26hetero-oligomerHHblitsX-ray2.77Å0.250.11MRNA CLEAVAGE AND POLYADENYLATION FACTOR CLP1
2npi.1.A10.42hetero-oligomerHHblitsX-ray2.95Å0.250.09Protein CLP1
3kbq.1.A25.58homo-dimerHHblitsX-ray2.00Å0.320.08Protein Ta0487
3kbq.1.B25.58homo-dimerHHblitsX-ray2.00Å0.320.08Protein Ta0487
3te6.1.A6.67monomerHHblitsX-ray2.80Å0.230.09Regulatory protein SIR3
3te6.2.A6.67monomerHHblitsX-ray2.80Å0.230.09Regulatory protein SIR3
4f7w.1.B23.08homo-dimerHHblitsX-ray2.10Å0.320.08Pantothenate kinase
4f7w.1.A23.08homo-dimerHHblitsX-ray2.10Å0.320.08Pantothenate kinase
4f7w.3.A23.08homo-dimerHHblitsX-ray2.10Å0.320.08Pantothenate kinase
4f7w.4.B23.08homo-dimerHHblitsX-ray2.10Å0.320.08Pantothenate kinase
4ne2.2.A23.08homo-dimerHHblitsX-ray1.90Å0.320.08Pantothenate kinase
5b3f.1.A19.51homo-dimerHHblitsX-ray2.50Å0.270.08Phosphoribulokinase/uridine kinase
5b3f.1.B19.51homo-dimerHHblitsX-ray2.50Å0.270.08Phosphoribulokinase/uridine kinase
1sq5.1.A23.68homo-dimerHHblitsX-ray2.20Å0.320.07Pantothenate kinase
3syn.2.A29.73hetero-oligomerHHblitsX-ray3.06Å0.340.07Flagellar biosynthesis protein flhF
2px0.1.B29.73homo-dimerHHblitsX-ray3.00Å0.340.07Flagellar biosynthesis protein flhF
2px0.3.B29.73homo-dimerHHblitsX-ray3.00Å0.340.07Flagellar biosynthesis protein flhF
2px0.4.A29.73homo-dimerHHblitsX-ray3.00Å0.340.07Flagellar biosynthesis protein flhF
2px3.1.A29.73homo-dimerHHblitsX-ray3.20Å0.340.07Flagellar biosynthesis protein flhF
2px0.1.A29.73homo-dimerHHblitsX-ray3.00Å0.340.07Flagellar biosynthesis protein flhF
2g0t.1.A29.73homo-dimerHHblitsX-ray2.67Å0.320.07conserved hypothetical protein
5l3s.1.B27.03hetero-oligomerHHblitsX-ray1.90Å0.320.07Signal recognition particle receptor FtsY
5l3s.2.B27.03hetero-oligomerHHblitsX-ray1.90Å0.320.07Signal recognition particle receptor FtsY
5l3s.3.B27.03hetero-oligomerHHblitsX-ray1.90Å0.320.07Signal recognition particle receptor FtsY
5l3s.4.B27.03hetero-oligomerHHblitsX-ray1.90Å0.320.07Signal recognition particle receptor FtsY
5l3w.1.A27.03monomerHHblitsX-ray2.40Å0.320.07Signal recognition particle receptor FtsY
2p65.1.A17.95monomerHHblitsX-ray1.70Å0.270.08Hypothetical protein PF08_0063
4c7o.1.A21.62hetero-oligomerHHblitsX-ray2.60Å0.300.07SIGNAL RECOGNITION PARTICLE PROTEIN
4c7o.2.A21.62hetero-oligomerHHblitsX-ray2.60Å0.300.07SIGNAL RECOGNITION PARTICLE PROTEIN
5l3s.1.A27.78hetero-oligomerHHblitsX-ray1.90Å0.320.07Signal recognition particle 54 kDa protein
5l3s.4.A27.78hetero-oligomerHHblitsX-ray1.90Å0.320.07Signal recognition particle 54 kDa protein
1xjc.1.A15.79monomerHHblitsX-ray2.10Å0.270.07MobB protein homolog
1p9n.1.A21.62homo-dimerHHblitsX-ray2.80Å0.290.07Molybdopterin-guanine dinucleotide biosynthesis protein B
1p9n.1.B21.62homo-dimerHHblitsX-ray2.80Å0.290.07Molybdopterin-guanine dinucleotide biosynthesis protein B
1np6.1.A21.62homo-dimerHHblitsX-ray1.90Å0.290.07Molybdopterin-guanine dinucleotide biosynthesis protein B
1np6.1.B21.62homo-dimerHHblitsX-ray1.90Å0.290.07Molybdopterin-guanine dinucleotide biosynthesis protein B
4ue5.1.D31.43hetero-oligomerHHblitsEM9.00Å0.340.07SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN
2og2.1.A21.62monomerHHblitsX-ray2.00Å0.290.07Putative signal recognition particle receptor
1j8m.1.A27.78monomerHHblitsX-ray2.00Å0.310.07SIGNAL RECOGNITION 54 KDA PROTEIN
4pfs.1.A18.92monomerHHblitsX-ray2.30Å0.290.07Cobyrinic Acid a,c-diamide synthase
4pfs.2.A18.92monomerHHblitsX-ray2.30Å0.290.07Cobyrinic Acid a,c-diamide synthase
4ixn.1.A19.44homo-dimerHHblitsX-ray2.05Å0.300.07Uncharacterized GTP-binding protein YjiA
3kl4.1.A28.57hetero-oligomerHHblitsX-ray3.50Å0.320.07Signal recognition 54 kDa protein
1zu5.1.A19.44monomerHHblitsX-ray2.40Å0.300.07ftsY
1zu4.1.A19.44monomerHHblitsX-ray1.95Å0.300.07ftsY
5gad.1.722.22hetero-oligomerHHblitsEMNA0.300.07Signal recognition particle protein Ffh
2xxa.1.A22.22hetero-oligomerHHblitsX-ray3.94Å0.300.07SIGNAL RECOGNITION PARTICLE PROTEIN
2xxa.2.A22.22hetero-oligomerHHblitsX-ray3.94Å0.300.07SIGNAL RECOGNITION PARTICLE PROTEIN
2j28.1.H22.22hetero-oligomerHHblitsEM8.00Å0.300.07SIGNAL RECOGNITION PARTICLE 54
5gaf.1.722.22hetero-oligomerHHblitsEMNA0.300.07Signal recognition particle protein
3jaj.45.A32.35monomerHHblitsEMNA0.340.07SRP54
3jan.45.A32.35monomerHHblitsEMNA0.340.07SRP54
1rj9.1.B22.22hetero-oligomerHHblitsX-ray1.90Å0.300.07Signal recognition particle protein
5bwk.1.A25.71hetero-oligomerHHblitsX-ray6.00Å0.320.07ATPase GET3
5bw8.1.B25.71hetero-oligomerHHblitsX-ray2.80Å0.320.07ATPase GET3
5bw8.1.A25.71hetero-oligomerHHblitsX-ray2.80Å0.320.07ATPase GET3
5l3r.1.B22.22hetero-oligomerHHblitsX-ray2.50Å0.290.07Cell division protein FtsY homolog, chloroplastic
3b9q.1.A22.22monomerHHblitsX-ray1.75Å0.290.07Chloroplast SRP receptor homolog, alpha subunit CPFTSY
5if9.1.A19.44monomerHHblitsX-ray1.80Å0.290.07Cobyrinic Acid a,c-diamide synthase
5l3r.1.A22.22hetero-oligomerHHblitsX-ray2.50Å0.290.07Signal recognition particle 54 kDa protein, chloroplastic
3bfv.1.A22.86monomerHHblitsX-ray1.80Å0.310.07Membrane protein CapA1, Protein tyrosine kinase
4jmp.1.A22.86monomerHHblitsX-ray1.30Å0.310.07C-terminal fragment of CapA, Protein tyrosine kinase
3dm9.1.A22.22homo-hexamerHHblitsX-ray2.20Å0.290.07Signal recognition particle receptor
3e70.1.A22.22monomerHHblitsX-ray1.97Å0.290.07Signal recognition particle receptor
3dmd.1.F22.22homo-hexamerHHblitsX-ray2.21Å0.290.07Signal recognition particle receptor
3dmd.1.E22.22homo-hexamerHHblitsX-ray2.21Å0.290.07Signal recognition particle receptor
2bek.1.A29.41homo-dimerHHblitsX-ray1.80Å0.330.07SEGREGATION PROTEIN
1wcv.1.A29.41homo-dimerHHblitsX-ray1.60Å0.330.07SEGREGATION PROTEIN
2bej.1.A29.41homo-dimerHHblitsX-ray2.10Å0.330.07SEGREGATION PROTEIN
4ixm.2.B29.41homo-dimerHHblitsX-ray2.57Å0.330.07Uncharacterized GTP-binding protein YjiA
1nij.1.A29.41monomerHHblitsX-ray2.00Å0.330.07Hypothetical protein yjiA
1j8y.1.A25.71monomerHHblitsX-ray2.00Å0.300.07SIGNAL RECOGNITION 54 KDA PROTEIN
5nco.1.922.86hetero-oligomerHHblitsEM4.80Å0.300.07Signal recognition particle protein,Signal recognition particle protein,Signal recognition particle protein,Signal recognition particle protein,Signal recognition particle protein,Signal recognition particle protein,Signal recognition particle protein,Signal recognition particle protein,Signal recognition particle protein,Signal recognition particle protein
1vma.1.A19.44monomerHHblitsX-ray1.60Å0.280.07cell division protein FtsY
2ng1.1.A22.86monomerHHblitsX-ray2.02Å0.300.07SIGNAL SEQUENCE RECOGNITION PROTEIN FFH
2ffh.1.A22.86monomerHHblitsX-ray3.20Å0.300.07PROTEIN (FFH)
2j7p.1.A22.86hetero-oligomerHHblitsX-ray1.97Å0.300.07SIGNAL RECOGNITION PARTICLE PROTEIN
3ng1.1.A22.86monomerHHblitsX-ray2.30Å0.300.07SIGNAL SEQUENCE RECOGNITION PROTEIN FFH
2cnw.1.A22.86hetero-oligomerHHblitsX-ray2.39Å0.300.07SIGNAL RECOGNITION PARTICLE PROTEIN
2cnw.3.A22.86hetero-oligomerHHblitsX-ray2.39Å0.300.07SIGNAL RECOGNITION PARTICLE PROTEIN
2xkv.1.A22.86hetero-oligomerHHblitsEM13.50Å0.300.07SIGNAL RECOGNITION PARTICLE PROTEIN
4jlv.1.A20.00monomerHHblitsX-ray2.20Å0.300.07C-terminal fragment of Membrane protein CapA1, Putative uncharacterized protein capB1
2ved.1.A20.00homo-octamerHHblitsX-ray2.60Å0.300.07MEMBRANE PROTEIN CAPA1, PROTEIN TYROSINE KINASE
3la6.1.F17.65homo-octamerHHblitsX-ray3.20Å0.320.07Tyrosine-protein kinase wzc
3la6.1.B17.65homo-octamerHHblitsX-ray3.20Å0.320.07Tyrosine-protein kinase wzc
3la6.1.C17.65homo-octamerHHblitsX-ray3.20Å0.320.07Tyrosine-protein kinase wzc
3la6.1.D17.65homo-octamerHHblitsX-ray3.20Å0.320.07Tyrosine-protein kinase wzc
3la6.1.E17.65homo-octamerHHblitsX-ray3.20Å0.320.07Tyrosine-protein kinase wzc
3la6.1.A17.65homo-octamerHHblitsX-ray3.20Å0.320.07Tyrosine-protein kinase wzc
3la6.1.G17.65homo-octamerHHblitsX-ray3.20Å0.320.07Tyrosine-protein kinase wzc
3la6.1.H17.65homo-octamerHHblitsX-ray3.20Å0.320.07Tyrosine-protein kinase wzc
3la6.2.C17.65homo-octamerHHblitsX-ray3.20Å0.320.07Tyrosine-protein kinase wzc
5u1g.1.A33.33hetero-oligomerHHblitsX-ray3.64Å0.340.06ParA
5u1g.2.B33.33hetero-oligomerHHblitsX-ray3.64Å0.340.06ParA
1fts.1.A19.44monomerHHblitsX-ray2.20Å0.270.07FTSY
4ak9.1.A16.67homo-dimerHHblitsX-ray1.80Å0.270.07CPFTSY
3ez7.1.A11.43homo-dimerHHblitsX-ray2.92Å0.290.07Plasmid partition protein A
3ez6.1.A11.43homo-dimerHHblitsX-ray2.58Å0.290.07Plasmid partition protein A
3ez6.1.B11.43homo-dimerHHblitsX-ray2.58Å0.290.07Plasmid partition protein A
3ez2.1.B11.43homo-dimerHHblitsX-ray2.05Å0.290.07Plasmid partition protein A
5j1j.1.A26.47homo-dimerHHblitsX-ray1.55Å0.310.07Site-determining protein
5j1j.1.B26.47homo-dimerHHblitsX-ray1.55Å0.310.07Site-determining protein
5jvf.1.A26.47monomerHHblitsX-ray1.66Å0.310.07Site-determining protein
1a7j.1.A23.53monomerHHblitsX-ray2.50Å0.310.07PHOSPHORIBULOKINASE
4nkr.1.A16.67homo-dimerHHblitsX-ray2.41Å0.270.07Molybdopterin-guanine dinucleotide biosynthesis protein B
4nkr.2.A16.67homo-dimerHHblitsX-ray2.41Å0.270.07Molybdopterin-guanine dinucleotide biosynthesis protein B
4nkr.2.B16.67homo-dimerHHblitsX-ray2.41Å0.270.07Molybdopterin-guanine dinucleotide biosynthesis protein B
4nkr.3.A16.67homo-dimerHHblitsX-ray2.41Å0.270.07Molybdopterin-guanine dinucleotide biosynthesis protein B
4nkr.3.B16.67homo-dimerHHblitsX-ray2.41Å0.270.07Molybdopterin-guanine dinucleotide biosynthesis protein B
2cnw.1.B17.14hetero-oligomerHHblitsX-ray2.39Å0.290.07CELL DIVISION PROTEIN FTSY
2iyl.1.A17.14monomerHHblitsX-ray2.10Å0.290.07CELL DIVISION PROTEIN FTSY
2cnw.2.B17.14hetero-oligomerHHblitsX-ray2.39Å0.290.07CELL DIVISION PROTEIN FTSY
5l3q.1.B17.14hetero-oligomerHHblitsX-ray3.20Å0.290.07Signal recognition particle receptor subunit alpha
2c03.1.A23.53monomerHHblitsX-ray1.24Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
2c03.2.A23.53monomerHHblitsX-ray1.24Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
1ffh.1.A23.53monomerHHblitsX-ray2.05Å0.310.07FFH
2j45.1.A23.53monomerHHblitsX-ray1.14Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
2j45.2.A23.53monomerHHblitsX-ray1.14Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
2j46.1.A23.53monomerHHblitsX-ray1.14Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
2j46.2.A23.53monomerHHblitsX-ray1.14Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
1o87.1.A23.53monomerHHblitsX-ray2.10Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
1o87.2.A23.53monomerHHblitsX-ray2.10Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
2c04.1.A23.53monomerHHblitsX-ray1.15Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
2c04.2.A23.53monomerHHblitsX-ray1.15Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
1ls1.1.A23.53monomerHHblitsX-ray1.10Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
1jpj.1.A23.53monomerHHblitsX-ray2.30Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
1jpn.1.A23.53monomerHHblitsX-ray1.90Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
1jpn.2.A23.53monomerHHblitsX-ray1.90Å0.310.07SIGNAL RECOGNITION PARTICLE PROTEIN
3dm5.1.A17.65homo-tetramerHHblitsX-ray2.51Å0.310.07Signal recognition 54 kDa protein
3fmi.1.A20.59homo-dimerHHblitsX-ray2.18Å0.310.07Dethiobiotin synthetase
3fmi.1.B20.59homo-dimerHHblitsX-ray2.18Å0.310.07Dethiobiotin synthetase
3fmf.2.A20.59homo-dimerHHblitsX-ray2.05Å0.310.07Dethiobiotin synthetase
3ez9.1.A17.14homo-dimerHHblitsX-ray2.80Å0.280.07ParA
3ez9.2.A17.14homo-dimerHHblitsX-ray2.80Å0.280.07ParA
3ezf.1.A17.14homo-dimerHHblitsX-ray2.80Å0.280.07ParA
1ion.1.A24.24monomerHHblitsX-ray2.30Å0.330.06PROBABLE CELL DIVISION INHIBITOR MIND
3of5.1.A23.53homo-dimerHHblitsX-ray1.52Å0.300.07Dethiobiotin synthetase
1g3r.1.A24.24monomerHHblitsX-ray2.70Å0.330.06CELL DIVISION INHIBITOR
4v02.1.A30.30hetero-oligomerHHblitsX-ray2.70Å0.330.06SITE-DETERMINING PROTEIN
5gad.1.920.00hetero-oligomerHHblitsEMNA0.280.07Signal recognition particle receptor FtsY
2yhs.1.A20.00monomerHHblitsX-ray1.60Å0.280.07CELL DIVISION PROTEIN FTSY
2xxa.1.B20.00hetero-oligomerHHblitsX-ray3.94Å0.280.07SRP RECEPTOR FTSY
2qy9.1.A20.00monomerHHblitsX-ray1.90Å0.280.07Cell division protein ftsY
4c7o.1.B20.00hetero-oligomerHHblitsX-ray2.60Å0.280.07SIGNAL RECOGNITION PARTICLE RECEPTOR FTSY
3c8u.1.A17.65monomerHHblitsX-ray1.95Å0.300.07Fructokinase
4e07.1.A34.38monomerHHblitsX-ray2.90Å0.350.06Plasmid partitioning protein ParF
4e09.1.A34.38homo-dimerHHblitsX-ray2.99Å0.350.06Plasmid partitioning protein ParF
4e03.1.A34.38monomerHHblitsX-ray2.45Å0.350.06Plasmid partitioning protein ParF
4e03.2.A34.38monomerHHblitsX-ray2.45Å0.350.06Plasmid partitioning protein ParF
4dzz.1.A34.38monomerHHblitsX-ray1.80Å0.350.06Plasmid partitioning protein ParF
4dzz.2.A34.38monomerHHblitsX-ray1.80Å0.350.06Plasmid partitioning protein ParF
5aun.1.B20.59hetero-oligomerHHblitsX-ray1.63Å0.300.07ATPase involved in chromosome partitioning, ParA/MinD family, Mrp homolog
3vx3.1.A20.59homo-dimerHHblitsX-ray2.10Å0.300.07ATPase involved in chromosome partitioning, ParA/MinD family, Mrp homolog
5auq.3.A20.59homo-dimerHHblitsX-ray2.53Å0.300.07ATPase involved in chromosome partitioning, ParA/MinD family, Mrp homolog
3vx3.1.B20.59homo-dimerHHblitsX-ray2.10Å0.300.07ATPase involved in chromosome partitioning, ParA/MinD family, Mrp homolog
1yr6.1.A31.25homo-dimerHHblitsX-ray2.15Å0.340.06ATP(GTP)binding protein
1yr7.1.A31.25homo-dimerHHblitsX-ray2.08Å0.340.06ATP(GTP)binding protein
1yr8.1.A31.25homo-dimerHHblitsX-ray2.40Å0.340.06ATP(GTP)binding protein
1yr9.1.A31.25homo-dimerHHblitsX-ray2.80Å0.340.06ATP(GTP)binding protein
1yra.1.A31.25homo-dimerHHblitsX-ray2.30Å0.340.06ATP(GTP)binding protein
1yra.1.B31.25homo-dimerHHblitsX-ray2.30Å0.340.06ATP(GTP)binding protein
1yrb.1.A31.25homo-dimerHHblitsX-ray1.75Å0.340.06ATP(GTP)binding protein
2oxr.1.A31.25homo-dimerHHblitsX-ray2.40Å0.340.06ATP(GTP)binding protein
3r9i.1.B31.25hetero-oligomerHHblitsX-ray2.60Å0.340.06Septum site-determining protein minD
3q9l.1.A31.25homo-dimerHHblitsX-ray2.34Å0.340.06Septum site-determining protein minD
4rz3.1.A23.53homo-dimerHHblitsX-ray1.90Å0.290.07Site-determining protein
4rz3.1.B23.53homo-dimerHHblitsX-ray1.90Å0.290.07Site-determining protein
4rz2.1.A23.53monomerHHblitsX-ray2.80Å0.290.07Site-determining protein
1dts.1.A30.30homo-dimerHHblitsX-ray1.65Å0.320.06DETHIOBIOTIN SYNTHETASE
1dah.1.A30.30homo-dimerHHblitsX-ray1.64Å0.320.06DETHIOBIOTIN SYNTHETASE
1byi.1.A30.30homo-dimerHHblitsX-ray0.97Å0.320.06DETHIOBIOTIN SYNTHASE
4v03.1.A27.27homo-dimerHHblitsX-ray1.90Å0.310.06SITE-DETERMINING PROTEIN
4ohv.1.A17.14monomerHHblitsX-ray2.30Å0.270.07Protein clpf-1
4oyh.1.A17.14homo-dimerHHblitsX-ray2.41Å0.270.07Molybdopterin-guanine dinucleotide biosynthesis protein B
4oyh.2.A17.14homo-dimerHHblitsX-ray2.41Å0.270.07Molybdopterin-guanine dinucleotide biosynthesis protein B
4oyh.2.B17.14homo-dimerHHblitsX-ray2.41Å0.270.07Molybdopterin-guanine dinucleotide biosynthesis protein B
4oyh.3.A17.14homo-dimerHHblitsX-ray2.41Å0.270.07Molybdopterin-guanine dinucleotide biosynthesis protein B
4oyh.3.B17.14homo-dimerHHblitsX-ray2.41Å0.270.07Molybdopterin-guanine dinucleotide biosynthesis protein B
2j7p.1.B17.65hetero-oligomerHHblitsX-ray1.97Å0.290.07CELL DIVISION PROTEIN FTSY
1okk.1.B17.65hetero-oligomerHHblitsX-ray2.05Å0.290.07CELL DIVISION PROTEIN FTSY
2xkv.1.D17.65hetero-oligomerHHblitsEM13.50Å0.290.07CELL DIVISION PROTEIN FTSY
2q9a.1.A17.65monomerHHblitsX-ray2.24Å0.290.07Cell division protein ftsY
2q9a.2.A17.65monomerHHblitsX-ray2.24Å0.290.07Cell division protein ftsY
3ug7.1.A23.53homo-tetramerHHblitsX-ray2.90Å0.290.07arsenical pump-driving ATPase
3ug6.1.A23.53homo-tetramerHHblitsX-ray3.30Å0.290.07arsenical pump-driving ATPase
3ea0.1.A14.71homo-dimerHHblitsX-ray2.20Å0.290.07ATPase, ParA family
3ea0.1.B14.71homo-dimerHHblitsX-ray2.20Å0.290.07ATPase, ParA family
2xj9.1.A27.27homo-dimerHHblitsX-ray2.80Å0.310.06MIPZ
2xj9.1.B27.27homo-dimerHHblitsX-ray2.80Å0.310.06MIPZ
3fwy.1.A15.15homo-dimerHHblitsX-ray1.63Å0.300.06Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
3fwy.1.B15.15homo-dimerHHblitsX-ray1.63Å0.300.06Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
1hyq.1.A21.21monomerHHblitsX-ray2.60Å0.300.06CELL DIVISION INHIBITOR (MIND-1)
3ibg.1.A28.13homo-dimerHHblitsX-ray3.20Å0.330.06ATPase, subunit of the Get complex
2ph1.1.A21.21homo-dimerHHblitsX-ray2.70Å0.300.06Nucleotide-binding protein
2oze.1.A21.88homo-dimerHHblitsX-ray1.83Å0.320.06Orf delta'
3mle.1.A32.26homo-dimerHHblitsX-ray2.80Å0.340.06Dethiobiotin synthetase
1odf.1.A20.59monomerHHblitsX-ray2.25Å0.270.07HYPOTHETICAL 33.3 KDA PROTEIN IN ADE3-SER2 INTERGENIC REGION
3cr7.1.A28.13homo-dimerHHblitsX-ray2.50Å0.310.06Adenylyl-sulfate kinase
3cr7.1.B28.13homo-dimerHHblitsX-ray2.50Å0.310.06Adenylyl-sulfate kinase
1e2e.1.A28.13homo-dimerHHblitsX-ray2.00Å0.300.06THYMIDYLATE KINASE
3kb1.1.A18.18homo-dimerHHblitsX-ray2.90Å0.280.06Nucleotide-binding protein
4twg.1.B21.88homo-trimerHHblitsX-ray1.85Å0.300.06Molybdopterin biosynthesis Mog protein
4twg.1.A21.88homo-trimerHHblitsX-ray1.85Å0.300.06Molybdopterin biosynthesis Mog protein
4twg.1.C21.88homo-trimerHHblitsX-ray1.85Å0.300.06Molybdopterin biosynthesis Mog protein
1g20.1.E18.75hetero-oligomerHHblitsX-ray2.20Å0.300.06NITROGENASE IRON PROTEIN
1g21.1.H18.75hetero-oligomerHHblitsX-ray3.00Å0.300.06NITROGENASE IRON PROTEIN
1g21.1.E18.75hetero-oligomerHHblitsX-ray3.00Å0.300.06NITROGENASE IRON PROTEIN
4rfv.1.A25.81homo-dimerHHblitsX-ray1.69Å0.320.06Bifunctional enzyme CysN/CysC
3n2i.1.A25.00homo-dimerHHblitsX-ray2.25Å0.290.06Thymidylate kinase
3ld9.1.A26.67homo-tetramerHHblitsX-ray2.15Å0.330.06Thymidylate kinase
2ax4.1.A22.58homo-dimerHHblitsX-ray2.50Å0.300.06Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2
2hly.1.A12.90monomerHHblitsX-ray1.60Å0.290.06Hypothetical protein Atu2299
1m7h.4.B26.67homo-tetramerHHblitsX-ray2.00Å0.320.06Adenylylsulfate kinase
1d6j.1.B26.67homo-dimerHHblitsX-ray2.00Å0.320.06ADENOSINE-5'PHOSPHOSULFATE KINASE
1d6j.1.A26.67homo-dimerHHblitsX-ray2.00Å0.320.06ADENOSINE-5'PHOSPHOSULFATE KINASE
1m7h.4.C26.67homo-tetramerHHblitsX-ray2.00Å0.320.06Adenylylsulfate kinase
1m7g.5.A26.67homo-tetramerHHblitsX-ray1.43Å0.320.06Adenylylsulfate kinase
3v9p.1.A30.00monomerHHblitsX-ray1.90Å0.310.06Thymidylate kinase
4bzq.1.A26.67homo-dimerHHblitsX-ray2.10Å0.310.06BIFUNCTIONAL ENZYME CYSN/CYSC
5cb6.3.B26.67homo-dimerHHblitsX-ray2.79Å0.310.06Probable adenylyl-sulfate kinase
5cb6.2.B26.67homo-dimerHHblitsX-ray2.79Å0.310.06Probable adenylyl-sulfate kinase
5bq5.1.A30.00monomerHHblitsX-ray2.10Å0.310.06Insertion sequence IS5376 putative ATP-binding protein
3uxm.1.A19.35monomerHHblitsX-ray1.95Å0.280.06Thymidylate kinase
3uxm.2.A19.35monomerHHblitsX-ray1.95Å0.280.06Thymidylate kinase
3ecc.1.A26.67monomerHHblitsX-ray2.70Å0.300.06DNA replication protein DnaC
2yvu.1.A27.59homo-dimerHHblitsX-ray2.10Å0.320.06Probable adenylyl-sulfate kinase
2yvu.1.B27.59homo-dimerHHblitsX-ray2.10Å0.320.06Probable adenylyl-sulfate kinase
1de0.1.A20.00homo-dimerHHblitsX-ray2.40Å0.290.06NITROGENASE IRON PROTEIN
1xcp.1.A20.00homo-dimerHHblitsX-ray3.20Å0.290.06Nitrogenase iron protein 1
1xcp.2.A20.00homo-dimerHHblitsX-ray3.20Å0.290.06Nitrogenase iron protein 1
1m34.1.E20.00hetero-oligomerHHblitsX-ray2.30Å0.290.06Nitrogenase Iron Protein 1
1m1y.1.E20.00hetero-oligomerHHblitsX-ray3.20Å0.290.06nitrogenase IRON protein 1
1m1y.1.F20.00hetero-oligomerHHblitsX-ray3.20Å0.290.06nitrogenase IRON protein 1
2afi.1.E20.00hetero-oligomerHHblitsX-ray3.10Å0.290.06Nitrogenase iron protein 1
2afh.1.E20.00hetero-oligomerHHblitsX-ray2.10Å0.290.06Nitrogenase iron protein 1
2afh.1.F20.00hetero-oligomerHHblitsX-ray2.10Å0.290.06Nitrogenase iron protein 1
1g5p.1.A20.00homo-dimerHHblitsX-ray2.20Å0.290.06NITROGENASE IRON PROTEIN
1g5p.1.B20.00homo-dimerHHblitsX-ray2.20Å0.290.06NITROGENASE IRON PROTEIN
1g1m.1.A20.00homo-dimerHHblitsX-ray2.25Å0.290.06NITROGENASE IRON PROTEIN
1g1m.1.B20.00homo-dimerHHblitsX-ray2.25Å0.290.06NITROGENASE IRON PROTEIN
1fp6.1.A20.00homo-dimerHHblitsX-ray2.15Å0.290.06NITROGENASE IRON PROTEIN
1nip.1.A20.00homo-dimerHHblitsX-ray2.90Å0.290.06NITROGENASE IRON PROTEIN
1nip.1.B20.00homo-dimerHHblitsX-ray2.90Å0.290.06NITROGENASE IRON PROTEIN
2ofw.1.B27.59homo-dimerHHblitsX-ray2.05Å0.300.06APS kinase domain of the PAPS synthetase 1
2ofw.1.A27.59homo-dimerHHblitsX-ray2.05Å0.300.06APS kinase domain of the PAPS synthetase 1
3uwo.1.A16.67monomerHHblitsX-ray1.70Å0.270.06Thymidylate kinase
1xd9.1.A20.69homo-dimerHHblitsX-ray2.80Å0.290.06Nitrogenase iron protein 1
1xdb.1.A20.69homo-dimerHHblitsX-ray2.80Å0.290.06Nitrogenase iron protein 1
2pbr.1.B35.71homo-dimerHHblitsX-ray1.96Å0.320.06Thymidylate kinase
2pbr.1.A35.71homo-dimerHHblitsX-ray1.96Å0.320.06Thymidylate kinase
4s35.1.B35.71homo-dimerHHblitsX-ray1.55Å0.320.06Thymidylate kinase
5xb2.1.B35.71homo-dimerHHblitsX-ray2.16Å0.320.06Thymidylate kinase
4wzb.1.F21.43hetero-oligomerHHblitsX-ray2.30Å0.300.06Nitrogenase iron protein 1
4wzb.1.E21.43hetero-oligomerHHblitsX-ray2.30Å0.300.06Nitrogenase iron protein 1
4wza.1.E21.43hetero-oligomerHHblitsX-ray1.90Å0.300.06Nitrogenase iron protein 1
4wza.1.F21.43hetero-oligomerHHblitsX-ray1.90Å0.300.06Nitrogenase iron protein 1
3tqc.1.A30.77homo-dimerHHblitsX-ray2.30Å0.350.05Pantothenate kinase
5he9.1.A17.24hetero-oligomerHHblitsX-ray1.90Å0.260.06Helicase loader
5he8.2.B17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.2.A17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.6.B17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.3.B17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.3.A17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.6.A17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.5.A17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.5.B17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.1.A17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.4.A17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.4.B17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
5he8.1.B17.24homo-dimerHHblitsX-ray2.60Å0.260.06Helicase loader
3avo.1.A25.93homo-dimerHHblitsX-ray2.55Å0.310.05Pantothenate kinase
3avp.1.A25.93homo-dimerHHblitsX-ray2.60Å0.310.05Pantothenate kinase
2get.1.A25.93homo-dimerHHblitsX-ray2.35Å0.310.05Pantothenate kinase
2geu.1.A25.93homo-dimerHHblitsX-ray2.90Å0.310.05Pantothenate kinase
4bft.1.A25.93homo-dimerHHblitsX-ray2.29Å0.310.05PANTOTHENATE KINASE
4bfs.1.A25.93homo-dimerHHblitsX-ray2.90Å0.310.05PANTOTHENATE KINASE
4bft.1.B25.93homo-dimerHHblitsX-ray2.29Å0.310.05PANTOTHENATE KINASE
4bfu.1.B25.93homo-dimerHHblitsX-ray2.28Å0.310.05PANTOTHENATE KINASE
4bfw.1.B25.93homo-dimerHHblitsX-ray2.27Å0.310.05PANTOTHENATE KINASE
1esm.1.A26.92homo-dimerHHblitsX-ray2.50Å0.330.05PANTOTHENATE KINASE
1esm.1.B26.92homo-dimerHHblitsX-ray2.50Å0.330.05PANTOTHENATE KINASE
1esn.1.A26.92homo-dimerHHblitsX-ray2.60Å0.330.05PANTOTHENATE KINASE
1esn.1.B26.92homo-dimerHHblitsX-ray2.60Å0.330.05PANTOTHENATE KINASE
1esn.2.B26.92homo-dimerHHblitsX-ray2.60Å0.330.05PANTOTHENATE KINASE
3pzy.1.A26.92homo-trimerHHblitsX-ray1.80Å0.330.05Mog
1cp2.1.A17.86homo-dimerHHblitsX-ray1.93Å0.270.06NITROGENASE IRON PROTEIN
1cp2.1.B17.86homo-dimerHHblitsX-ray1.93Å0.270.06NITROGENASE IRON PROTEIN
4ba6.1.A19.23monomerHHblitsX-ray1.42Å0.310.05ENDOGLUCANASE CEL5A
5afe.1.A19.23monomerHHblitsX-ray2.60Å0.310.05ENDOGLUCANASE CEL5A
2ypj.1.A19.23monomerHHblitsX-ray2.35Å0.310.05ENDOGLUCANASE CEL5A
4bzp.1.A32.00homo-dimerHHblitsX-ray1.47Å0.340.05BIFUNCTIONAL ENZYME CYSN/CYSC
2qsy.1.A41.67monomerHHblitsX-ray1.95Å0.370.05Nicotinamide riboside kinase 1
2qt0.1.A41.67monomerHHblitsX-ray1.92Å0.370.05Nicotinamide riboside kinase 1
1p9r.1.A33.33monomerHHblitsX-ray2.50Å0.330.05General secretion pathway protein E
3uie.1.A33.33homo-dimerHHblitsX-ray1.79Å0.330.05Adenylyl-sulfate kinase 1, chloroplastic
4aek.1.A20.83monomerHHblitsX-ray1.75Å0.320.05ENDOGLUCANASE CEL5A
4aem.1.A20.83monomerHHblitsX-ray2.10Å0.320.05ENDOGLUCANASE CEL5A
2eyu.1.A29.17monomerHHblitsX-ray1.87Å0.320.05twitching motility protein PilT
2eyu.2.A29.17monomerHHblitsX-ray1.87Å0.320.05twitching motility protein PilT
1s96.1.A11.54homo-dimerHHblitsX-ray2.00Å0.250.05Guanylate kinase
1in6.1.A34.78monomerHHblitsX-ray1.80Å0.340.05HOLLIDAY JUNCTION DNA HELICASE RUVB
4ksr.1.A34.78homo-hexamerHHblitsX-ray4.20Å0.340.05Type II secretion system protein E, Hemolysin-coregulated protein
4ksr.1.B34.78homo-hexamerHHblitsX-ray4.20Å0.340.05Type II secretion system protein E, Hemolysin-coregulated protein
4ksr.1.C34.78homo-hexamerHHblitsX-ray4.20Å0.340.05Type II secretion system protein E, Hemolysin-coregulated protein
3ec2.1.A34.78monomerHHblitsX-ray2.70Å0.340.05DNA replication protein DnaC
4ttq.1.A36.36monomerHHblitsX-ray2.20Å0.370.04Dephospho-CoA kinase
4ttp.1.A36.36monomerHHblitsX-ray2.20Å0.370.04Dephospho-CoA kinase
2qg6.1.A40.91monomerHHblitsX-ray1.50Å0.370.04Nicotinamide riboside kinase 1
4gfd.1.A34.78homo-dimerHHblitsX-ray1.80Å0.330.05Thymidylate kinase
2cck.1.B34.78homo-dimerHHblitsX-ray2.21Å0.330.05THYMIDYLATE KINASE
1jbk.1.A29.17monomerHHblitsX-ray1.80Å0.290.05CLPB PROTEIN
5ujm.1.D20.83hetero-oligomerHHblitsEMNA0.280.05Origin recognition complex subunit 4
5uj7.2.B20.83hetero-oligomerHHblitsX-ray3.39Å0.280.05Origin recognition complex subunit 4
1xex.1.A17.39hetero-oligomerHHblitsX-ray2.50Å0.300.05SMC protein
1xew.1.A17.39hetero-oligomerHHblitsX-ray2.00Å0.300.05SMC protein
3kta.1.A17.39hetero-oligomerHHblitsX-ray1.63Å0.300.05Chromosome segregation protein smc
3kta.2.A17.39hetero-oligomerHHblitsX-ray1.63Å0.300.05Chromosome segregation protein smc
1z6g.1.A16.67monomerHHblitsX-ray2.18Å0.250.05guanylate kinase