SWISS-MODEL Homology Modelling Report

Model Building Report

This document lists the results for the homology modelling project "T5D7W9-MurB-H-pylori" submitted to SWISS-MODEL workspace on Oct. 17, 2017, 3:39 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 149 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
None
0.69-3.41
QMEAN-3.41
-1.72
All Atom-2.07
Solvation-0.76
Torsion-2.97
TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityRangeCoverageDescription
4pyt.1.A30.08monomerHHblitsX-ray1.85Å0.36 4 - 259 0.99UDP-N-acetylenolpyruvoylglucosamine reductase
LigandAdded to ModelDescription
CL✕ - Not biologically relevant.
CHLORIDE ION
CL✕ - Not biologically relevant.
CHLORIDE ION
FAD✕ - Binding site not conserved.
FLAVIN-ADENINE DINUCLEOTIDE
MG✕ - Not biologically relevant.
MAGNESIUM ION
MG✕ - Not biologically relevant.
MAGNESIUM ION
MG✕ - Not biologically relevant.
MAGNESIUM ION

Target    MLETIIDFSRYSSVKIGVPLKVSVLENDDEI-----------SQEHQIIGLANNLLIAPG-AKNLALLG-KNYDYICDKG
4pyt.1.A ---ENEPLANHTTIKIGGPADCLVIPKDIQAVRDTMEVVKNHGVQWRAIGRGSNLLVLDEGIRGVVIKLGAGLDHMEIDG

Target ECIEIGGAANSSKIFNYFRANDLGGLEFLGQLPGTLGALVKMNAGMKEFEIKNVLESACI-----NNQWLGSGALGLDYR
4pyt.1.A EQVTVGGGYSVVRLSTGISKKGLSGLEFASGIPGSVGGAVYMNAGAHGSDISRILVKALILFEDGTMEWLTNEEMEFSYR

Target SSKFKG----VVLRARFKKTLGFREGV---LKACKSMRK-SHP-KLPNFGSCFKNPPNDYAGRLLEGVGLRGYCLKRVGF
4pyt.1.A TSILQNKRPGICLEAVLQLEQKERDAIVAQMQKNKDYRKETQPVSNPCAGSIFRNPLPDHAGRLVEQAGLKGHRIGGAKV

Target AKEHANFLVNLGGAEFEEALDLIELAKTRVLQEYGIHLEEEVKILR
4pyt.1.A SEMHGNFIVNAGGATAKDVLDLIAFIQKTIKEKYDIDMHTEVEIVG




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 8 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 141 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.

MLETIIDFSRYSSVKIGVPLKVSVLENDDEISQEHQIIGLANNLLIAPGAKNLALLGKNYDYICDKGECIEIGGAANSSKIFNYFRANDLGGLEFLGQLP
GTLGALVKMNAGMKEFEIKNVLESACINNQWLGSGALGLDYRSSKFKGVVLRARFKKTLGFREGVLKACKSMRKSHPKLPNFGSCFKNPPNDYAGRLLEG
VGLRGYCLKRVGFAKEHANFLVNLGGAEFEEALDLIELAKTRVLQEYGIHLEEEVKILR

Table T2:

TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityCoverageDescription
4pyt.1.A30.08monomerHHblitsX-ray1.85Å0.360.99UDP-N-acetylenolpyruvoylglucosamine reductase
4pyt.1.A32.27monomerBLASTX-ray1.85Å0.370.97UDP-N-acetylenolpyruvoylglucosamine reductase
3tx1.1.A33.33monomerBLASTX-ray2.69Å0.360.96UDP-N-acetylenolpyruvoylglucosamine reductase
3tx1.1.A30.20monomerHHblitsX-ray2.69Å0.340.98UDP-N-acetylenolpyruvoylglucosamine reductase
1hsk.1.A28.13monomerHHblitsX-ray2.30Å0.340.99UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE
4jay.1.A27.73monomerHHblitsX-ray2.23Å0.320.99UDP-N-acetylenolpyruvoylglucosamine reductase
4jb1.1.A27.73monomerHHblitsX-ray2.10Å0.320.99UDP-N-acetylenolpyruvoylglucosamine reductase
3i99.1.A24.90monomerHHblitsX-ray2.20Å0.310.99UDP-N-acetylenolpyruvoylglucosamine reductase
5jzx.1.A23.74homo-dimerHHblitsX-ray2.20Å0.310.99UDP-N-acetylenolpyruvoylglucosamine reductase
5jzx.1.B23.74homo-dimerHHblitsX-ray2.20Å0.310.99UDP-N-acetylenolpyruvoylglucosamine reductase
2mbr.1.A23.32monomerHHblitsX-ray1.80Å0.320.98URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1uxy.1.A22.92monomerHHblitsX-ray1.80Å0.320.98URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1mbb.1.A22.44monomerHHblitsX-ray2.30Å0.310.98URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1mbt.1.A22.44monomerHHblitsX-ray3.00Å0.310.98URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
2q85.1.A22.44monomerHHblitsX-ray2.51Å0.310.98UDP-N-acetylenolpyruvoylglucosamine reductase
2gqu.1.A27.13monomerHHblitsX-ray1.60Å0.330.95UDP-N-Acetylenolpyruvylglucosamine Reductase
2gqt.1.A27.13monomerHHblitsX-ray1.30Å0.330.95UDP-N-Acetylenolpyruvylglucosamine Reductase
1hsk.1.A32.13monomerBLASTX-ray2.30Å0.360.85UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE
4jay.1.A32.26monomerBLASTX-ray2.23Å0.340.84UDP-N-acetylenolpyruvoylglucosamine reductase
4jb1.1.A32.26monomerBLASTX-ray2.10Å0.340.84UDP-N-acetylenolpyruvoylglucosamine reductase
2gqu.1.A34.98monomerBLASTX-ray1.60Å0.380.78UDP-N-Acetylenolpyruvylglucosamine Reductase
2gqt.1.A34.98monomerBLASTX-ray1.30Å0.380.78UDP-N-Acetylenolpyruvylglucosamine Reductase
3i99.1.A35.33monomerBLASTX-ray2.20Å0.370.71UDP-N-acetylenolpyruvoylglucosamine reductase
4f4q.1.A16.67monomerHHblitsX-ray2.62Å0.280.58DprE1
4aut.1.A16.67monomerHHblitsX-ray2.10Å0.280.58DECAPRENYL-PHOSPHORYL-BETA-D-RIBOFURANOSE-2-OXIDOREDUCTASE
3pm9.1.A14.84homo-dimerHHblitsX-ray2.57Å0.250.60Putative oxidoreductase
2vfs.1.A15.17monomerHHblitsX-ray1.60Å0.280.56XYLITOL OXIDASE
4fdp.1.A15.28monomerHHblitsX-ray2.23Å0.270.56oxidoreductase DprE1
4fdp.2.A15.28monomerHHblitsX-ray2.23Å0.270.56oxidoreductase DprE1
4ncr.1.A15.28monomerHHblitsX-ray1.88Å0.270.56decaprenylphosphoryl-beta-D-ribose oxidase
1w1k.1.A14.97homo-dimerHHblitsX-ray2.55Å0.250.57VANILLYL-ALCOHOL OXIDASE
5mxu.1.A14.97homo-octamerHHblitsX-ray2.80Å0.250.57Vanillyl-alcohol oxidase
4p8c.1.A15.28monomerHHblitsX-ray1.95Å0.270.56Probable decaprenylphosphoryl-beta-D-ribose oxidase
4p8c.2.A15.28monomerHHblitsX-ray1.95Å0.270.56Probable decaprenylphosphoryl-beta-D-ribose oxidase
4p8m.1.A15.28monomerHHblitsX-ray2.09Å0.270.56Probable decaprenylphosphoryl-beta-D-ribose oxidase
1w1m.1.A14.97homo-dimerHHblitsX-ray3.00Å0.250.57VANILLYL-ALCOHOL OXIDASE
1i19.1.A13.10monomerHHblitsX-ray1.70Å0.260.56CHOLESTEROL OXIDASE
1ahv.1.A14.29homo-octamerHHblitsX-ray3.10Å0.250.57VANILLYL-ALCOHOL OXIDASE
1ahu.1.A14.29homo-octamerHHblitsX-ray2.70Å0.250.57VANILLYL-ALCOHOL OXIDASE
4kw5.1.A15.38monomerHHblitsX-ray2.61Å0.270.55Oxidoreductase
2uuu.1.A11.56homo-dimerHHblitsX-ray1.95Å0.250.57ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE
2uuv.2.B11.56homo-dimerHHblitsX-ray1.99Å0.250.57ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE
1e8g.1.A14.38homo-octamerHHblitsX-ray2.10Å0.250.56VANILLYL-ALCOHOL OXIDASE
3js8.1.A11.72monomerHHblitsX-ray1.54Å0.260.56Cholesterol oxidase
1dzn.1.A13.61homo-octamerHHblitsX-ray2.80Å0.250.57VANILLYL-ALCOHOL OXIDASE
1w1j.1.A14.38homo-dimerHHblitsX-ray2.70Å0.250.56VANILLYL-ALCOHOL OXIDASE
3b9j.1.B8.16hetero-oligomerHHblitsX-ray2.30Å0.240.57xanthine oxidase
1fiq.1.B8.16hetero-oligomerHHblitsX-ray2.50Å0.240.57XANTHINE OXIDASE
2axr.1.A11.56monomerHHblitsX-ray1.98Å0.240.57glucooligosaccharide oxidase
4ml8.1.A9.52monomerHHblitsX-ray2.70Å0.240.57Cytokinin oxidase 2
3hsu.1.A11.64monomerHHblitsX-ray1.69Å0.240.56Glucooligosaccharide oxidase
3nvv.1.B8.22hetero-oligomerHHblitsX-ray1.82Å0.240.56Xanthine dehydrogenase/oxidase
2e3t.1.A8.28homo-dimerHHblitsX-ray2.28Å0.250.56Xanthine dehydrogenase/oxidase
2e3t.1.B8.28homo-dimerHHblitsX-ray2.28Å0.250.56Xanthine dehydrogenase/oxidase
1wyg.1.A7.59monomerHHblitsX-ray2.60Å0.250.56Xanthine dehydrogenase/oxidase
4ytz.1.A7.59homo-dimerHHblitsX-ray2.30Å0.250.56Xanthine dehydrogenase/oxidase
4ytz.1.B7.59homo-dimerHHblitsX-ray2.30Å0.250.56Xanthine dehydrogenase/oxidase
4ysw.1.B7.59homo-dimerHHblitsX-ray1.99Å0.250.56Xanthine dehydrogenase/oxidase
4o95.1.A8.90monomerHHblitsX-ray1.75Å0.240.56Cytokinin dehydrogenase 4
5hhz.1.A8.90monomerHHblitsX-ray2.00Å0.240.56Cytokinin dehydrogenase 4
5epg.1.A7.53homo-dimerHHblitsX-ray3.39Å0.240.56Aldehyde oxidase
2i0k.1.A11.89monomerHHblitsX-ray1.60Å0.260.55Oxidoreductase
4bc7.1.A11.11homo-dimerHHblitsX-ray2.40Å0.250.56ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL
4bby.1.A11.11homo-dimerHHblitsX-ray1.90Å0.250.56ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL
3sr6.1.B8.28hetero-oligomerHHblitsX-ray2.10Å0.240.56Xanthine dehydrogenase/oxidase
5fxd.1.A10.34homo-dimerHHblitsX-ray1.70Å0.240.56PROBABLE VANILLYL-ALCOHOL OXIDASE
3uni.1.A8.33homo-dimerHHblitsX-ray2.20Å0.240.56Xanthine dehydrogenase/oxidase
4bca.1.A11.19homo-dimerHHblitsX-ray2.40Å0.250.55ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL
2ckj.1.A6.21homo-dimerHHblitsX-ray3.59Å0.240.56XANTHINE OXIDOREDUCTASE
5k8e.1.A11.03monomerHHblitsX-ray1.93Å0.240.56FAD linked oxidase-like protein
2e1q.1.A6.21homo-dimerHHblitsX-ray2.60Å0.240.56Xanthine dehydrogenase/oxidase
3pqb.1.A14.18homo-dimerHHblitsX-ray2.32Å0.260.54Putative oxidoreductase
4uhw.1.A6.90homo-dimerHHblitsX-ray2.60Å0.240.56ALDEHYDE OXIDASE
2bvg.1.A13.89monomerHHblitsX-ray3.18Å0.240.566-HYDROXY-D-NICOTINE OXIDASE
1diq.1.A11.03hetero-oligomerHHblitsX-ray2.75Å0.230.56P-CRESOL METHYLHYDROXYLASE
3w8w.1.A13.79homo-dimerHHblitsX-ray1.95Å0.230.56Putative FAD-dependent oxygenase EncM
1w1q.1.A10.49monomerHHblitsX-ray1.80Å0.240.55CYTOKININ DEHYDROGENASE 1
3s1d.1.A10.49monomerHHblitsX-ray1.75Å0.240.55Cytokinin dehydrogenase 1
3vte.1.A10.49monomerHHblitsX-ray2.75Å0.240.55Tetrahydrocannabinolic acid synthase
4xlo.1.A13.10homo-dimerHHblitsX-ray1.67Å0.230.56FAD-dependent oxygenase EncM
3s1f.1.A10.56monomerHHblitsX-ray2.00Å0.240.55Cytokinin dehydrogenase 1
3s1e.1.A10.56monomerHHblitsX-ray1.90Å0.240.55Cytokinin dehydrogenase 1
3fwa.1.A9.86monomerHHblitsX-ray1.50Å0.240.55Reticuline oxidase
1wve.1.A10.42hetero-oligomerHHblitsX-ray1.85Å0.230.564-cresol dehydrogenase [hydroxylating] flavoprotein subunit
4pzf.1.A9.86monomerHHblitsX-ray2.20Å0.240.55Reticuline oxidase
2w3r.1.A14.49hetero-oligomerHHblitsX-ray2.90Å0.260.53XANTHINE DEHYDROGENASE
2q4w.1.A10.49monomerHHblitsX-ray1.70Å0.230.55Cytokinin dehydrogenase 7
1jro.1.A14.49hetero-oligomerHHblitsX-ray2.70Å0.260.53xanthine dehydrogenase, chain A
3fw9.1.A9.15monomerHHblitsX-ray1.49Å0.240.55Reticuline oxidase
3d2j.1.A9.93monomerHHblitsX-ray2.05Å0.240.54berberine bridge-forming enzyme
3rj8.1.A6.21monomerHHblitsX-ray2.40Å0.220.56Carbohydrate oxidase
3fw8.1.A9.93monomerHHblitsX-ray1.50Å0.240.54Reticuline oxidase
3gsy.1.A9.93monomerHHblitsX-ray1.63Å0.240.54Reticuline oxidase; Berberine bridge-forming enzyme
2qpm.1.A10.64monomerHHblitsX-ray1.85Å0.240.54Cytokinin dehydrogenase 1
3kjm.1.A10.64monomerHHblitsX-ray1.90Å0.240.54Cytokinin dehydrogenase 1
3dq0.1.A10.64monomerHHblitsX-ray1.90Å0.240.54Cytokinin dehydrogenase 1
4ec3.1.A9.93monomerHHblitsX-ray2.65Å0.240.54Reticuline oxidase
4pve.1.A7.69monomerHHblitsX-ray1.50Å0.230.55Pollen allergen Phl p 4.0202
4pvk.1.A7.69monomerHHblitsX-ray1.30Å0.230.55Pollen allergen Phl p 4.0202
3fw7.1.A9.93monomerHHblitsX-ray1.82Å0.240.54Reticuline oxidase
3tsh.1.A8.45monomerHHblitsX-ray1.90Å0.230.55Pollen allergen Phl p 4
4dns.1.A8.39monomerHHblitsX-ray2.15Å0.230.55FAD-linked oxidoreductase BG60
4pvh.1.A7.75monomerHHblitsX-ray1.40Å0.230.55Pollen allergen Phl p 4.0202
4pvj.1.A7.80monomerHHblitsX-ray1.80Å0.230.54Pollen allergen Phl p 4.0202
5d79.1.A9.15monomerHHblitsX-ray1.85Å0.220.55Berberine bridge enzyme-like protein
5i1v.1.A8.63homo-dimerHHblitsX-ray1.84Å0.240.54CrmK
2ipi.1.A8.63monomerHHblitsX-ray1.65Å0.240.54Aclacinomycin oxidoreductase (AknOx)
2y3r.1.A8.63homo-dimerHHblitsX-ray1.79Å0.240.54TAML
4ud8.1.A7.75monomerHHblitsX-ray2.09Å0.220.55FAD-BINDING AND BBE DOMAIN-CONTAINING PROTEIN
4ud8.2.A7.75monomerHHblitsX-ray2.09Å0.220.55FAD-BINDING AND BBE DOMAIN-CONTAINING PROTEIN
2wdw.1.A8.63homo-dimerHHblitsX-ray3.21Å0.230.54PUTATIVE HEXOSE OXIDASE
5awv.1.C8.63homo-tetramerHHblitsX-ray1.93Å0.230.54Putative hexose oxidase
4zoh.1.B13.64hetero-oligomerHHblitsX-ray2.20Å0.260.51Putative oxidoreductase FAD-binding subunit
1ffu.1.C10.61hetero-oligomerHHblitsX-ray2.35Å0.240.51CUTM, FLAVOPROTEIN OF CARBON MONOXIDE DEHYDROGENASE
3hrd.1.C13.01hetero-oligomerHHblitsX-ray2.20Å0.270.47Nicotinate dehydrogenase FAD-subunit
1n62.1.C8.94hetero-oligomerHHblitsX-ray1.09Å0.240.47Carbon monoxide dehydrogenase medium chain
1zxi.1.C8.94hetero-oligomerHHblitsX-ray1.70Å0.240.47Carbon monoxide dehydrogenase medium chain
1ffv.1.C11.48hetero-oligomerHHblitsX-ray2.25Å0.250.47CUTM, FLAVOPROTEIN OF CARBON MONOXIDE DEHYDROGENASE
1t3q.1.C11.57hetero-oligomerHHblitsX-ray1.80Å0.250.47quinoline 2-oxidoreductase medium subunit
1qlt.1.A14.41homo-octamerHHblitsX-ray2.20Å0.250.46VANILLYL-ALCOHOL OXIDASE
5mxj.1.A13.56homo-octamerHHblitsX-ray2.80Å0.250.46Vanillyl-alcohol oxidase
1w1l.1.A12.82homo-dimerHHblitsX-ray2.70Å0.240.45VANILLYL-ALCOHOL OXIDASE
1e0y.1.A12.82homo-dimerHHblitsX-ray2.75Å0.240.45VANILLYL-ALCOHOL OXIDASE
4g3t.1.A17.76monomerHHblitsX-ray2.35Å0.290.41oxidoreductase DprE1
1f0x.1.A6.93monomerHHblitsX-ray1.90Å0.220.39D-LACTATE DEHYDROGENASE
2yvs.1.A16.13homo-dimerHHblitsX-ray2.00Å0.260.36Glycolate oxidase subunit GlcE
2yvs.1.B16.13homo-dimerHHblitsX-ray2.00Å0.260.36Glycolate oxidase subunit GlcE
1m1b.1.A10.20homo-tetramerHHblitsX-ray2.25Å0.290.19PHOSPHOENOLPYRUVATE PHOSPHOMUTASE
1s2v.1.A10.20homo-tetramerHHblitsX-ray2.10Å0.290.19Phosphoenolpyruvate phosphomutase
1s2w.1.A10.20monomerHHblitsX-ray1.69Å0.290.19Phosphoenolpyruvate phosphomutase
2ze3.1.A20.41homo-dimerHHblitsX-ray1.65Å0.280.19DFA0005
1s2u.1.A10.20homo-tetramerHHblitsX-ray2.00Å0.280.19Phosphoenolpyruvate phosphomutase
3m0k.1.A12.24homo-tetramerHHblitsX-ray1.65Å0.270.19Oxaloacetate acetylhydrolase
5unc.1.A18.37homo-tetramerHHblitsX-ray1.71Å0.270.19PHOSPHOENOLPYRUVATE PHOSPHOMUTASE
4iqd.1.A14.29homo-dimerHHblitsX-ray2.00Å0.270.19Carboxyvinyl-carboxyphosphonate phosphorylmutase
4iqe.1.B14.29homo-dimerHHblitsX-ray2.50Å0.270.19Carboxyvinyl-carboxyphosphonate phosphorylmutase
2hjp.1.A12.24homo-tetramerHHblitsX-ray1.90Å0.270.19Phosphonopyruvate hydrolase
1zlp.1.A10.42homo-tetramerHHblitsX-ray2.70Å0.270.19petal death protein
3n4w.1.B8.70homo-dimerHHblitsX-ray1.45Å0.260.18Receptor-type tyrosine-protein phosphatase-like N
3n4w.1.A8.70homo-dimerHHblitsX-ray1.45Å0.260.18Receptor-type tyrosine-protein phosphatase-like N
3np5.1.A8.70homo-tetramerHHblitsX-ray1.80Å0.260.18Receptor-type tyrosine-protein phosphatase-like N
3n01.1.A8.70homo-dimerHHblitsX-ray1.30Å0.260.18Receptor-type tyrosine-protein phosphatase-like N
3n01.1.B8.70homo-dimerHHblitsX-ray1.30Å0.260.18Receptor-type tyrosine-protein phosphatase-like N
3np5.1.B8.70homo-tetramerHHblitsX-ray1.80Å0.260.18Receptor-type tyrosine-protein phosphatase-like N
3np5.1.D8.70homo-tetramerHHblitsX-ray1.80Å0.260.18Receptor-type tyrosine-protein phosphatase-like N
2qt7.1.A8.89homo-tetramerHHblitsX-ray1.30Å0.260.17Receptor-type tyrosine-protein phosphatase-like N
2qt7.1.B8.89homo-tetramerHHblitsX-ray1.30Å0.260.17Receptor-type tyrosine-protein phosphatase-like N
4hti.1.A13.95monomerHHblitsX-ray1.95Å0.270.17Receptor-type tyrosine-protein phosphatase N2
4htj.1.A13.95monomerHHblitsX-ray2.01Å0.270.17Receptor-type tyrosine-protein phosphatase N2