SWISS-MODEL Homology Modelling Report

Model Building Report

This document lists the results for the homology modelling project "A0A086BTX7-MurB-P-aeruginosa" submitted to SWISS-MODEL workspace on Oct. 17, 2017, 3:43 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 146 templates were found (Table T2).

Models

The following model was built (see Materials and Methods "Model Building"):

Model #01

FileBuilt withOligo-StateLigandsGMQEQMEAN
PDB ProMod3 Version 1.0.2. MONOMER
1 x B3P: 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL;
1 x K: POTASSIUM ION;
1 x NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
0.970.53
QMEAN0.53
1.65
All Atom1.31
Solvation0.69
Torsion0.03
TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityRangeCoverageDescription
4jay.1.A90.27monomerHHblitsX-ray2.23Å0.57 2 - 339 1.00UDP-N-acetylenolpyruvoylglucosamine reductase
LigandAdded to ModelDescription
B3P
2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
K
POTASSIUM ION
NAP
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
FAD✕ - Binding site not conserved.
FLAVIN-ADENINE DINUCLEOTIDE

Target    MSLELQEQCSLKPYNSFGIDVRARLLAHARGEADVREALALARQRSLPLLVIGGGSNLLLTRDVEALVLRMASQGRRILS
4jay.1.A MSLELQEHCSLKPYNTFGIDVRARLLAHARDEADVREALALARERGLPLLVIGGGSNLLLTRDVEALVLRMASQGRRIVS

Target EADDMVLVEAEAGETWDPFVQWSLEQGLAGLENLSLIPGTVGAAPMQNIGAYGVELKDVFDSLTALDRQDGSLREFDREA
4jay.1.A DAADSVLVEAEAGEAWDPFVQWSLERGLAGLENLSLIPGTVGAAPMQNIGAYGVELKDVFDSLTALDRQDGTLREFDRQA

Target CRFGYRDSLFKQEPDRWLILRVRLRLSRRSGLHLDYGPVRQRLQEEGIANPTAQDVSRVICAIRREKLPDPAVLGNAGSF
4jay.1.A CRFGYRDSLFKQEPDRWLILRVRLRLTRRERLHLDYGPVRQRLEEEGIASPTARDVSRVICAIRREKLPDPAVLGNAGSF

Target FKNPLVSATQAAMLRRTYPDLVAYPQADGQVKLAAGWLIDKGGWKGFRDGPVGVHAQQALVLVNHGGASGAQVQALAERI
4jay.1.A FKNPLVDATQAERLRQAFPDLVGYPQADGRLKLAAGWLIDKGGWKGFRDGPVGVHAQQALVLVNHGGATGAQVRALAERI

Target QADVRQRFGVELEREPNLY
4jay.1.A QEDVRRRFGVELEPEPNLY




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 15 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 133 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.

MSLELQEQCSLKPYNSFGIDVRARLLAHARGEADVREALALARQRSLPLLVIGGGSNLLLTRDVEALVLRMASQGRRILSEADDMVLVEAEAGETWDPFV
QWSLEQGLAGLENLSLIPGTVGAAPMQNIGAYGVELKDVFDSLTALDRQDGSLREFDREACRFGYRDSLFKQEPDRWLILRVRLRLSRRSGLHLDYGPVR
QRLQEEGIANPTAQDVSRVICAIRREKLPDPAVLGNAGSFFKNPLVSATQAAMLRRTYPDLVAYPQADGQVKLAAGWLIDKGGWKGFRDGPVGVHAQQAL
VLVNHGGASGAQVQALAERIQADVRQRFGVELEREPNLY

Table T2:

TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityCoverageDescription
4jay.1.A90.27monomerHHblitsX-ray2.23Å0.571.00UDP-N-acetylenolpyruvoylglucosamine reductase
4jb1.1.A90.27monomerHHblitsX-ray2.10Å0.571.00UDP-N-acetylenolpyruvoylglucosamine reductase
3i99.1.A44.11monomerHHblitsX-ray2.20Å0.410.98UDP-N-acetylenolpyruvoylglucosamine reductase
3i99.1.A44.65monomerBLASTX-ray2.20Å0.410.96UDP-N-acetylenolpyruvoylglucosamine reductase
1mbb.1.A44.04monomerHHblitsX-ray2.30Å0.400.96URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1mbt.1.A44.04monomerHHblitsX-ray3.00Å0.400.96URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
2q85.1.A44.04monomerHHblitsX-ray2.51Å0.400.96UDP-N-acetylenolpyruvoylglucosamine reductase
2mbr.1.A44.17monomerHHblitsX-ray1.80Å0.400.96URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1uxy.1.A43.87monomerHHblitsX-ray1.80Å0.400.96URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1mbb.1.A45.79monomerBLASTX-ray2.30Å0.400.95URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1mbt.1.A45.79monomerBLASTX-ray3.00Å0.400.95URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
2q85.1.A45.79monomerBLASTX-ray2.51Å0.400.95UDP-N-acetylenolpyruvoylglucosamine reductase
2mbr.1.A45.79monomerBLASTX-ray1.80Å0.400.95URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1uxy.1.A45.48monomerBLASTX-ray1.80Å0.400.95URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
5jzx.1.A35.95homo-dimerHHblitsX-ray2.20Å0.360.98UDP-N-acetylenolpyruvoylglucosamine reductase
5jzx.1.B35.95homo-dimerHHblitsX-ray2.20Å0.360.98UDP-N-acetylenolpyruvoylglucosamine reductase
5jzx.1.A40.57homo-dimerBLASTX-ray2.20Å0.380.83UDP-N-acetylenolpyruvoylglucosamine reductase
5jzx.1.B40.57homo-dimerBLASTX-ray2.20Å0.380.83UDP-N-acetylenolpyruvoylglucosamine reductase
3tx1.1.A31.88monomerBLASTX-ray2.69Å0.360.81UDP-N-acetylenolpyruvoylglucosamine reductase
3tx1.1.A28.47monomerHHblitsX-ray2.69Å0.340.83UDP-N-acetylenolpyruvoylglucosamine reductase
1hsk.1.A26.33monomerHHblitsX-ray2.30Å0.330.83UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE
4pyt.1.A26.24monomerHHblitsX-ray1.85Å0.330.83UDP-N-acetylenolpyruvoylglucosamine reductase
2gqu.1.A32.32monomerHHblitsX-ray1.60Å0.340.78UDP-N-Acetylenolpyruvylglucosamine Reductase
2gqt.1.A32.32monomerHHblitsX-ray1.30Å0.340.78UDP-N-Acetylenolpyruvylglucosamine Reductase
2gqu.1.A35.08monomerBLASTX-ray1.60Å0.360.73UDP-N-Acetylenolpyruvylglucosamine Reductase
2gqt.1.A35.08monomerBLASTX-ray1.30Å0.360.73UDP-N-Acetylenolpyruvylglucosamine Reductase
4pyt.1.A28.16monomerBLASTX-ray1.85Å0.350.72UDP-N-acetylenolpyruvoylglucosamine reductase
3pm9.1.A16.85homo-dimerHHblitsX-ray2.57Å0.270.53Putative oxidoreductase
4xlo.1.A20.24homo-dimerHHblitsX-ray1.67Å0.290.50FAD-dependent oxygenase EncM
3w8w.1.A20.36homo-dimerHHblitsX-ray1.95Å0.290.49Putative FAD-dependent oxygenase EncM
2vfs.1.A17.86monomerHHblitsX-ray1.60Å0.280.50XYLITOL OXIDASE
4f4q.1.A19.16monomerHHblitsX-ray2.62Å0.280.49DprE1
4aut.1.A19.16monomerHHblitsX-ray2.10Å0.280.49DECAPRENYL-PHOSPHORYL-BETA-D-RIBOFURANOSE-2-OXIDOREDUCTASE
4o95.1.A19.88monomerHHblitsX-ray1.75Å0.290.49Cytokinin dehydrogenase 4
5hhz.1.A19.88monomerHHblitsX-ray2.00Å0.290.49Cytokinin dehydrogenase 4
1w1m.1.A19.76homo-dimerHHblitsX-ray3.00Å0.280.49VANILLYL-ALCOHOL OXIDASE
1dzn.1.A19.76homo-octamerHHblitsX-ray2.80Å0.280.49VANILLYL-ALCOHOL OXIDASE
5mxu.1.A19.76homo-octamerHHblitsX-ray2.80Å0.280.49Vanillyl-alcohol oxidase
1e8g.1.A20.48homo-octamerHHblitsX-ray2.10Å0.280.49VANILLYL-ALCOHOL OXIDASE
2bvg.1.A17.96monomerHHblitsX-ray3.18Å0.280.496-HYDROXY-D-NICOTINE OXIDASE
1qlt.1.A20.48homo-octamerHHblitsX-ray2.20Å0.280.49VANILLYL-ALCOHOL OXIDASE
1ahv.1.A19.76homo-octamerHHblitsX-ray3.10Å0.280.49VANILLYL-ALCOHOL OXIDASE
1ahu.1.A19.76homo-octamerHHblitsX-ray2.70Å0.280.49VANILLYL-ALCOHOL OXIDASE
1w1k.1.A19.88homo-dimerHHblitsX-ray2.55Å0.280.49VANILLYL-ALCOHOL OXIDASE
2q4w.1.A19.39monomerHHblitsX-ray1.70Å0.280.49Cytokinin dehydrogenase 7
5mxj.1.A19.28homo-octamerHHblitsX-ray2.80Å0.280.49Vanillyl-alcohol oxidase
1i19.1.A18.79monomerHHblitsX-ray1.70Å0.280.49CHOLESTEROL OXIDASE
1w1j.1.A19.88homo-dimerHHblitsX-ray2.70Å0.280.49VANILLYL-ALCOHOL OXIDASE
2uuu.1.A13.69homo-dimerHHblitsX-ray1.95Å0.270.50ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE
2uuv.2.B13.69homo-dimerHHblitsX-ray1.99Å0.270.50ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE
4kw5.1.A18.56monomerHHblitsX-ray2.61Å0.270.49Oxidoreductase
1e0y.1.A18.67homo-dimerHHblitsX-ray2.75Å0.270.49VANILLYL-ALCOHOL OXIDASE
4ml8.1.A19.14monomerHHblitsX-ray2.70Å0.290.48Cytokinin oxidase 2
4bc7.1.A15.06homo-dimerHHblitsX-ray2.40Å0.270.49ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL
4bby.1.A15.06homo-dimerHHblitsX-ray1.90Å0.270.49ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL
4bca.1.A15.15homo-dimerHHblitsX-ray2.40Å0.270.49ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL
2i0k.1.A17.79monomerHHblitsX-ray1.60Å0.280.48Oxidoreductase
5fxd.1.A13.25homo-dimerHHblitsX-ray1.70Å0.270.49PROBABLE VANILLYL-ALCOHOL OXIDASE
1w1l.1.A16.97homo-dimerHHblitsX-ray2.70Å0.270.49VANILLYL-ALCOHOL OXIDASE
2axr.1.A15.24monomerHHblitsX-ray1.98Å0.270.48glucooligosaccharide oxidase
3js8.1.A19.63monomerHHblitsX-ray1.54Å0.270.48Cholesterol oxidase
1diq.1.A12.65hetero-oligomerHHblitsX-ray2.75Å0.260.49P-CRESOL METHYLHYDROXYLASE
1wve.1.A13.33hetero-oligomerHHblitsX-ray1.85Å0.260.494-cresol dehydrogenase [hydroxylating] flavoprotein subunit
2qpm.1.A16.67monomerHHblitsX-ray1.85Å0.270.48Cytokinin dehydrogenase 1
3kjm.1.A16.67monomerHHblitsX-ray1.90Å0.270.48Cytokinin dehydrogenase 1
3hsu.1.A14.81monomerHHblitsX-ray1.69Å0.270.48Glucooligosaccharide oxidase
3vte.1.A15.43monomerHHblitsX-ray2.75Å0.270.48Tetrahydrocannabinolic acid synthase
5k8e.1.A13.50monomerHHblitsX-ray1.93Å0.260.48FAD linked oxidase-like protein
3fw7.1.A14.11monomerHHblitsX-ray1.82Å0.260.48Reticuline oxidase
4fdp.1.A18.63monomerHHblitsX-ray2.23Å0.270.47oxidoreductase DprE1
4fdp.2.A18.63monomerHHblitsX-ray2.23Å0.270.47oxidoreductase DprE1
4ncr.1.A18.63monomerHHblitsX-ray1.88Å0.270.47decaprenylphosphoryl-beta-D-ribose oxidase
5i1v.1.A15.85homo-dimerHHblitsX-ray1.84Å0.260.48CrmK
3rj8.1.A12.88monomerHHblitsX-ray2.40Å0.260.48Carbohydrate oxidase
3pqb.1.A14.46homo-dimerHHblitsX-ray2.32Å0.240.49Putative oxidoreductase
4p8c.1.A18.75monomerHHblitsX-ray1.95Å0.270.47Probable decaprenylphosphoryl-beta-D-ribose oxidase
4p8c.2.A18.75monomerHHblitsX-ray1.95Å0.270.47Probable decaprenylphosphoryl-beta-D-ribose oxidase
4p8m.1.A18.75monomerHHblitsX-ray2.09Å0.270.47Probable decaprenylphosphoryl-beta-D-ribose oxidase
4dns.1.A13.58monomerHHblitsX-ray2.15Å0.260.48FAD-linked oxidoreductase BG60
4pzf.1.A14.20monomerHHblitsX-ray2.20Å0.260.48Reticuline oxidase
3s1e.1.A16.98monomerHHblitsX-ray1.90Å0.280.47Cytokinin dehydrogenase 1
3s1d.1.A16.98monomerHHblitsX-ray1.75Å0.280.47Cytokinin dehydrogenase 1
3dq0.1.A16.98monomerHHblitsX-ray1.90Å0.280.47Cytokinin dehydrogenase 1
3fw8.1.A13.58monomerHHblitsX-ray1.50Å0.260.48Reticuline oxidase
3s1f.1.A16.98monomerHHblitsX-ray2.00Å0.280.47Cytokinin dehydrogenase 1
3tsh.1.A11.73monomerHHblitsX-ray1.90Å0.260.48Pollen allergen Phl p 4
4pvk.1.A11.73monomerHHblitsX-ray1.30Å0.260.48Pollen allergen Phl p 4.0202
4pve.1.A11.11monomerHHblitsX-ray1.50Å0.260.48Pollen allergen Phl p 4.0202
4pvh.1.A11.11monomerHHblitsX-ray1.40Å0.260.48Pollen allergen Phl p 4.0202
4ud8.1.A16.15monomerHHblitsX-ray2.09Å0.260.47FAD-BINDING AND BBE DOMAIN-CONTAINING PROTEIN
4ud8.2.A16.15monomerHHblitsX-ray2.09Å0.260.47FAD-BINDING AND BBE DOMAIN-CONTAINING PROTEIN
1w1q.1.A15.63monomerHHblitsX-ray1.80Å0.270.47CYTOKININ DEHYDROGENASE 1
3fw9.1.A14.29monomerHHblitsX-ray1.49Å0.260.47Reticuline oxidase
3d2j.1.A14.29monomerHHblitsX-ray2.05Å0.260.47berberine bridge-forming enzyme
4pvj.1.A11.80monomerHHblitsX-ray1.80Å0.260.47Pollen allergen Phl p 4.0202
3fwa.1.A14.29monomerHHblitsX-ray1.50Å0.260.47Reticuline oxidase
3gsy.1.A14.29monomerHHblitsX-ray1.63Å0.260.47Reticuline oxidase; Berberine bridge-forming enzyme
4ec3.1.A14.38monomerHHblitsX-ray2.65Å0.260.47Reticuline oxidase
5d79.1.A14.29monomerHHblitsX-ray1.85Å0.260.47Berberine bridge enzyme-like protein
2wdw.1.A10.49homo-dimerHHblitsX-ray3.21Å0.250.48PUTATIVE HEXOSE OXIDASE
5awv.1.C10.49homo-tetramerHHblitsX-ray1.93Å0.250.48Putative hexose oxidase
3b9j.1.B10.06hetero-oligomerHHblitsX-ray2.30Å0.260.47xanthine oxidase
1n5x.1.A10.69homo-dimerHHblitsX-ray2.80Å0.260.47Xanthine Dehydrogenase
2y3r.1.A14.47homo-dimerHHblitsX-ray1.79Å0.260.47TAML
1fiq.1.B10.76hetero-oligomerHHblitsX-ray2.50Å0.260.47XANTHINE OXIDASE
5epg.1.A12.03homo-dimerHHblitsX-ray3.39Å0.260.47Aldehyde oxidase
4uhw.1.A12.03homo-dimerHHblitsX-ray2.60Å0.260.47ALDEHYDE OXIDASE
3amz.1.A10.06homo-dimerHHblitsX-ray2.10Å0.260.47Xanthine dehydrogenase/oxidase
3ax7.1.A10.06homo-dimerHHblitsX-ray2.34Å0.260.47Xanthine dehydrogenase/oxidase
3uni.1.A10.06homo-dimerHHblitsX-ray2.20Å0.260.47Xanthine dehydrogenase/oxidase
2ipi.1.A14.47monomerHHblitsX-ray1.65Å0.250.47Aclacinomycin oxidoreductase (AknOx)
3zyv.1.A10.06homo-dimerHHblitsX-ray2.55Å0.250.47AOX3
1hsk.1.A29.63monomerBLASTX-ray2.30Å0.360.40UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE
1n62.1.C16.00hetero-oligomerHHblitsX-ray1.09Å0.260.44Carbon monoxide dehydrogenase medium chain
1ffu.1.C14.77hetero-oligomerHHblitsX-ray2.35Å0.260.44CUTM, FLAVOPROTEIN OF CARBON MONOXIDE DEHYDROGENASE
1ffv.1.C14.86hetero-oligomerHHblitsX-ray2.25Å0.260.44CUTM, FLAVOPROTEIN OF CARBON MONOXIDE DEHYDROGENASE
1zxi.1.C12.75hetero-oligomerHHblitsX-ray1.70Å0.250.44Carbon monoxide dehydrogenase medium chain
4zoh.1.B12.93hetero-oligomerHHblitsX-ray2.20Å0.250.43Putative oxidoreductase FAD-binding subunit
1f0x.1.A11.63monomerHHblitsX-ray1.90Å0.240.38D-LACTATE DEHYDROGENASE
4g3t.1.A23.01monomerHHblitsX-ray2.35Å0.300.33oxidoreductase DprE1
2yvs.1.A14.85homo-dimerHHblitsX-ray2.00Å0.230.30Glycolate oxidase subunit GlcE
2yvs.1.B14.85homo-dimerHHblitsX-ray2.00Å0.230.30Glycolate oxidase subunit GlcE
4hti.1.A9.88monomerHHblitsX-ray1.95Å0.250.24Receptor-type tyrosine-protein phosphatase N2
4htj.1.A9.88monomerHHblitsX-ray2.01Å0.250.24Receptor-type tyrosine-protein phosphatase N2
1m1b.1.A22.45homo-tetramerHHblitsX-ray2.25Å0.300.14PHOSPHOENOLPYRUVATE PHOSPHOMUTASE
1s2v.1.A22.45homo-tetramerHHblitsX-ray2.10Å0.300.14Phosphoenolpyruvate phosphomutase
1s2w.1.A22.45monomerHHblitsX-ray1.69Å0.300.14Phosphoenolpyruvate phosphomutase
1s2u.1.A22.45homo-tetramerHHblitsX-ray2.00Å0.300.14Phosphoenolpyruvate phosphomutase
5unc.1.A14.29homo-tetramerHHblitsX-ray1.71Å0.280.14PHOSPHOENOLPYRUVATE PHOSPHOMUTASE
2hjp.1.A14.29homo-tetramerHHblitsX-ray1.90Å0.270.14Phosphonopyruvate hydrolase
4iqd.1.A14.29homo-dimerHHblitsX-ray2.00Å0.260.14Carboxyvinyl-carboxyphosphonate phosphorylmutase
4iqe.1.B14.29homo-dimerHHblitsX-ray2.50Å0.260.14Carboxyvinyl-carboxyphosphonate phosphorylmutase
3m0k.1.A14.29homo-tetramerHHblitsX-ray1.65Å0.240.14Oxaloacetate acetylhydrolase
2zv3.1.A13.16homo-dimerHHblitsX-ray2.10Å0.290.11Peptidyl-tRNA hydrolase
2zv3.3.B13.16homo-dimerHHblitsX-ray2.10Å0.290.11Peptidyl-tRNA hydrolase
2zv3.4.A13.16homo-dimerHHblitsX-ray2.10Å0.290.11Peptidyl-tRNA hydrolase
2zv3.4.B13.16homo-dimerHHblitsX-ray2.10Å0.290.11Peptidyl-tRNA hydrolase
1xty.1.A10.26homo-dimerHHblitsX-ray1.80Å0.270.12Peptidyl-tRNA hydrolase
1wn2.1.A13.16homo-dimerHHblitsX-ray1.20Å0.290.11Peptidyl-tRNA hydrolase
2d3k.1.A13.16homo-dimerHHblitsX-ray1.90Å0.290.11Peptidyl-tRNA hydrolase
1q7s.1.A15.79monomerHHblitsX-ray2.00Å0.270.11bit1
1q7s.2.A15.79monomerHHblitsX-ray2.00Å0.270.11bit1
1rlk.1.A7.89monomerHHblitsX-ray1.95Å0.270.11Hypothetical protein Ta0108
3erj.1.A5.26homo-dimerHHblitsX-ray1.80Å0.240.11Peptidyl-tRNA hydrolase
3erj.1.B5.26homo-dimerHHblitsX-ray1.80Å0.240.11Peptidyl-tRNA hydrolase
1rzw.1.A5.26monomerHHblitsNMRNA0.240.11Protein AF2095(GR4)