SWISS-MODEL Homology Modelling Report

Model Building Report

This document lists the results for the homology modelling project "G2JLK8-MurB-A-baumannii" submitted to SWISS-MODEL workspace on Oct. 17, 2017, 3:50 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 172 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
0.75-1.42
QMEAN-1.42
-0.63
All Atom-0.50
Solvation0.16
Torsion-1.34
TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityRangeCoverageDescription
4jay.1.A44.41monomerBLASTX-ray2.23Å0.42 9 - 342 0.94UDP-N-acetylenolpyruvoylglucosamine reductase
LigandAdded to ModelDescription
B3P✕ - Binding site not conserved.
2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
FAD✕ - Binding site not conserved.
FLAVIN-ADENINE DINUCLEOTIDE
K✕ - Binding site not conserved.
POTASSIUM ION
NAP✕ - Binding site not conserved.
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

Target    MFKNRFFNTMQIQNQVQLKPFNTLSLDVTASHYTKVKSIEDIEEALAFAKEHELNVLVLSGGSNMLLPQQINALVIHLDI
4jay.1.A --------SLELQEHCSLKPYNTFGIDVRARLLAHARDEADVREALALARERGLPLLVIGGGSNLLLTRDVEALVLRMAS

Target QGIDVLSEDQDFIRVKVGAGQVWHDFVLYSTKQNWFGLQNLALIPGLVGASPVQNIGAYGVEVGEFIESVQVYDRLLKQT
4jay.1.A QGRRIVSDAADSVLVEAEAGEAWDPFVQWSLERGLAGLENLSLIPGTVGAAPMQNIGAYGVELKDVFDSLTALDR---QD

Target GSISAAD---CHFSYRHSIFKDDPARYIITHVTFKLLKQANLKLNYGDLKQAVGD----NLTAENLQNQVIHIRQSKLPD
4jay.1.A GTLREFDRQACRFGYRDSLFKQEPDRWLILRVRLRLTRRERLHLDYGPVRQRLEEEGIASPTARDVSRVICAIRREKLPD

Target PKEYPNVGSFFKNPIVNTQEFERLIAQFSTIPHYPQANGNVKIAAGWLIDQAGWKGKQLGVVGMFHKQALVLVNYANASL
4jay.1.A PAVLGNAGSFFKNPLVDATQAERLRQAFPDLVGYPQADGRLKLAAGWLIDKGGWKGFRDGPVGVHAQQALVLVNHGGATG

Target ADVKKTYQAVQHDVEQRFQIMLEPEPVLYNNLGLIENHTE
4jay.1.A AQVRALAERIQEDVRRRFGVELEPEPNLY-----------




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 13 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 159 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.

MFKNRFFNTMQIQNQVQLKPFNTLSLDVTASHYTKVKSIEDIEEALAFAKEHELNVLVLSGGSNMLLPQQINALVIHLDIQGIDVLSEDQDFIRVKVGAG
QVWHDFVLYSTKQNWFGLQNLALIPGLVGASPVQNIGAYGVEVGEFIESVQVYDRLLKQTGSISAADCHFSYRHSIFKDDPARYIITHVTFKLLKQANLK
LNYGDLKQAVGDNLTAENLQNQVIHIRQSKLPDPKEYPNVGSFFKNPIVNTQEFERLIAQFSTIPHYPQANGNVKIAAGWLIDQAGWKGKQLGVVGMFHK
QALVLVNYANASLADVKKTYQAVQHDVEQRFQIMLEPEPVLYNNLGLIENHTE

Table T2:

TemplateSeq IdentityOligo-stateFound byMethodResolutionSeq SimilarityCoverageDescription
4jay.1.A44.41monomerBLASTX-ray2.23Å0.420.94UDP-N-acetylenolpyruvoylglucosamine reductase
4jb1.1.A44.41monomerBLASTX-ray2.10Å0.420.94UDP-N-acetylenolpyruvoylglucosamine reductase
4jay.1.A42.94monomerHHblitsX-ray2.23Å0.410.94UDP-N-acetylenolpyruvoylglucosamine reductase
4jb1.1.A42.94monomerHHblitsX-ray2.10Å0.410.94UDP-N-acetylenolpyruvoylglucosamine reductase
1mbb.1.A40.42monomerHHblitsX-ray2.30Å0.390.95URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1mbt.1.A40.42monomerHHblitsX-ray3.00Å0.390.95URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
2q85.1.A40.42monomerHHblitsX-ray2.51Å0.390.95UDP-N-acetylenolpyruvoylglucosamine reductase
2mbr.1.A40.54monomerHHblitsX-ray1.80Å0.390.94URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
3i99.1.A36.07monomerHHblitsX-ray2.20Å0.370.97UDP-N-acetylenolpyruvoylglucosamine reductase
1uxy.1.A40.24monomerHHblitsX-ray1.80Å0.390.94URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
5jzx.1.A37.84homo-dimerBLASTX-ray2.20Å0.380.94UDP-N-acetylenolpyruvoylglucosamine reductase
5jzx.1.B37.84homo-dimerBLASTX-ray2.20Å0.380.94UDP-N-acetylenolpyruvoylglucosamine reductase
3i99.1.A39.08monomerBLASTX-ray2.20Å0.390.92UDP-N-acetylenolpyruvoylglucosamine reductase
2mbr.1.A42.19monomerBLASTX-ray1.80Å0.400.91URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1mbb.1.A42.19monomerBLASTX-ray2.30Å0.400.91URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
1mbt.1.A42.19monomerBLASTX-ray3.00Å0.400.91URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
2q85.1.A42.19monomerBLASTX-ray2.51Å0.400.91UDP-N-acetylenolpyruvoylglucosamine reductase
1uxy.1.A41.88monomerBLASTX-ray1.80Å0.400.91URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
5jzx.1.A35.65homo-dimerHHblitsX-ray2.20Å0.360.94UDP-N-acetylenolpyruvoylglucosamine reductase
5jzx.1.B35.65homo-dimerHHblitsX-ray2.20Å0.360.94UDP-N-acetylenolpyruvoylglucosamine reductase
1hsk.1.A25.61monomerHHblitsX-ray2.30Å0.330.82UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE
3tx1.1.A26.15monomerHHblitsX-ray2.69Å0.340.80UDP-N-acetylenolpyruvoylglucosamine reductase
4pyt.1.A27.40monomerBLASTX-ray1.85Å0.340.80UDP-N-acetylenolpyruvoylglucosamine reductase
4pyt.1.A23.34monomerHHblitsX-ray1.85Å0.320.81UDP-N-acetylenolpyruvoylglucosamine reductase
1hsk.1.A32.09monomerBLASTX-ray2.30Å0.360.76UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE
3tx1.1.A33.87monomerBLASTX-ray2.69Å0.380.70UDP-N-acetylenolpyruvoylglucosamine reductase
2gqu.1.A27.27monomerHHblitsX-ray1.60Å0.320.75UDP-N-Acetylenolpyruvylglucosamine Reductase
2gqt.1.A27.27monomerHHblitsX-ray1.30Å0.320.75UDP-N-Acetylenolpyruvylglucosamine Reductase
3pm9.1.A16.76homo-dimerHHblitsX-ray2.57Å0.270.51Putative oxidoreductase
4f4q.1.A16.37monomerHHblitsX-ray2.62Å0.280.48DprE1
4aut.1.A16.37monomerHHblitsX-ray2.10Å0.280.48DECAPRENYL-PHOSPHORYL-BETA-D-RIBOFURANOSE-2-OXIDOREDUCTASE
4ml8.1.A13.45monomerHHblitsX-ray2.70Å0.280.48Cytokinin oxidase 2
1e8g.1.A16.07homo-octamerHHblitsX-ray2.10Å0.280.48VANILLYL-ALCOHOL OXIDASE
1ahv.1.A14.79homo-octamerHHblitsX-ray3.10Å0.270.48VANILLYL-ALCOHOL OXIDASE
1ahu.1.A14.79homo-octamerHHblitsX-ray2.70Å0.270.48VANILLYL-ALCOHOL OXIDASE
5mxu.1.A14.79homo-octamerHHblitsX-ray2.80Å0.270.48Vanillyl-alcohol oxidase
2uuu.1.A13.61homo-dimerHHblitsX-ray1.95Å0.270.48ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE
2uuv.2.B13.61homo-dimerHHblitsX-ray1.99Å0.270.48ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE
1w1m.1.A15.48homo-dimerHHblitsX-ray3.00Å0.270.48VANILLYL-ALCOHOL OXIDASE
1w1k.1.A15.48homo-dimerHHblitsX-ray2.55Å0.270.48VANILLYL-ALCOHOL OXIDASE
4p8c.1.A14.79monomerHHblitsX-ray1.95Å0.270.48Probable decaprenylphosphoryl-beta-D-ribose oxidase
4p8c.2.A14.79monomerHHblitsX-ray1.95Å0.270.48Probable decaprenylphosphoryl-beta-D-ribose oxidase
4p8m.1.A14.79monomerHHblitsX-ray2.09Å0.270.48Probable decaprenylphosphoryl-beta-D-ribose oxidase
1dzn.1.A15.48homo-octamerHHblitsX-ray2.80Å0.270.48VANILLYL-ALCOHOL OXIDASE
1w1j.1.A15.57homo-dimerHHblitsX-ray2.70Å0.270.47VANILLYL-ALCOHOL OXIDASE
4xlo.1.A19.63homo-dimerHHblitsX-ray1.67Å0.290.46FAD-dependent oxygenase EncM
3w8w.1.A19.63homo-dimerHHblitsX-ray1.95Å0.290.46Putative FAD-dependent oxygenase EncM
5fxd.1.A13.17homo-dimerHHblitsX-ray1.70Å0.270.47PROBABLE VANILLYL-ALCOHOL OXIDASE
2vfs.1.A18.63monomerHHblitsX-ray1.60Å0.290.46XYLITOL OXIDASE
2i0k.1.A14.63monomerHHblitsX-ray1.60Å0.280.46Oxidoreductase
2axr.1.A17.68monomerHHblitsX-ray1.98Å0.280.46glucooligosaccharide oxidase
1i19.1.A14.55monomerHHblitsX-ray1.70Å0.270.47CHOLESTEROL OXIDASE
2bvg.1.A18.40monomerHHblitsX-ray3.18Å0.280.466-HYDROXY-D-NICOTINE OXIDASE
1diq.1.A13.17hetero-oligomerHHblitsX-ray2.75Å0.260.47P-CRESOL METHYLHYDROXYLASE
1wve.1.A13.86hetero-oligomerHHblitsX-ray1.85Å0.270.474-cresol dehydrogenase [hydroxylating] flavoprotein subunit
4bby.1.A12.05homo-dimerHHblitsX-ray1.90Å0.270.47ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL
4bc7.1.A12.05homo-dimerHHblitsX-ray2.40Å0.270.47ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL
5k8e.1.A18.90monomerHHblitsX-ray1.93Å0.280.46FAD linked oxidase-like protein
3hsu.1.A17.79monomerHHblitsX-ray1.69Å0.280.46Glucooligosaccharide oxidase
4o95.1.A14.46monomerHHblitsX-ray1.75Å0.260.47Cytokinin dehydrogenase 4
5hhz.1.A14.46monomerHHblitsX-ray2.00Å0.260.47Cytokinin dehydrogenase 4
4bca.1.A12.12homo-dimerHHblitsX-ray2.40Å0.270.47ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL
4pve.1.A17.28monomerHHblitsX-ray1.50Å0.280.46Pollen allergen Phl p 4.0202
4kw5.1.A15.34monomerHHblitsX-ray2.61Å0.270.46Oxidoreductase
4pvk.1.A17.90monomerHHblitsX-ray1.30Å0.280.46Pollen allergen Phl p 4.0202
4pvh.1.A17.28monomerHHblitsX-ray1.40Å0.280.46Pollen allergen Phl p 4.0202
4pvj.1.A18.01monomerHHblitsX-ray1.80Å0.280.46Pollen allergen Phl p 4.0202
3tsh.1.A17.39monomerHHblitsX-ray1.90Å0.280.46Pollen allergen Phl p 4
4dns.1.A17.39monomerHHblitsX-ray2.15Å0.280.46FAD-linked oxidoreductase BG60
2q4w.1.A17.18monomerHHblitsX-ray1.70Å0.270.46Cytokinin dehydrogenase 7
3pqb.1.A16.67homo-dimerHHblitsX-ray2.32Å0.270.46Putative oxidoreductase
4fdp.1.A15.43monomerHHblitsX-ray2.23Å0.270.46oxidoreductase DprE1
4fdp.2.A15.43monomerHHblitsX-ray2.23Å0.270.46oxidoreductase DprE1
4ncr.1.A15.43monomerHHblitsX-ray1.88Å0.270.46decaprenylphosphoryl-beta-D-ribose oxidase
2qpm.1.A13.50monomerHHblitsX-ray1.85Å0.270.46Cytokinin dehydrogenase 1
3kjm.1.A13.50monomerHHblitsX-ray1.90Å0.270.46Cytokinin dehydrogenase 1
3dq0.1.A14.20monomerHHblitsX-ray1.90Å0.270.46Cytokinin dehydrogenase 1
3rj8.1.A14.63monomerHHblitsX-ray2.40Å0.260.46Carbohydrate oxidase
3js8.1.A10.98monomerHHblitsX-ray1.54Å0.260.46Cholesterol oxidase
4ud8.1.A14.20monomerHHblitsX-ray2.09Å0.260.46FAD-BINDING AND BBE DOMAIN-CONTAINING PROTEIN
4ud8.2.A14.20monomerHHblitsX-ray2.09Å0.260.46FAD-BINDING AND BBE DOMAIN-CONTAINING PROTEIN
4pzf.1.A16.05monomerHHblitsX-ray2.20Å0.260.46Reticuline oxidase
3d2j.1.A16.05monomerHHblitsX-ray2.05Å0.260.46berberine bridge-forming enzyme
3vte.1.A15.43monomerHHblitsX-ray2.75Å0.260.46Tetrahydrocannabinolic acid synthase
5d79.1.A18.63monomerHHblitsX-ray1.85Å0.270.46Berberine bridge enzyme-like protein
3fwa.1.A16.15monomerHHblitsX-ray1.50Å0.260.46Reticuline oxidase
1w1q.1.A13.66monomerHHblitsX-ray1.80Å0.260.46CYTOKININ DEHYDROGENASE 1
3s1e.1.A13.75monomerHHblitsX-ray1.90Å0.270.45Cytokinin dehydrogenase 1
3fw9.1.A15.63monomerHHblitsX-ray1.49Å0.270.45Reticuline oxidase
3s1f.1.A13.75monomerHHblitsX-ray2.00Å0.270.45Cytokinin dehydrogenase 1
3s1d.1.A13.04monomerHHblitsX-ray1.75Å0.260.46Cytokinin dehydrogenase 1
3fw7.1.A15.53monomerHHblitsX-ray1.82Å0.260.46Reticuline oxidase
1fiq.1.B10.06hetero-oligomerHHblitsX-ray2.50Å0.270.45XANTHINE OXIDASE
3gsy.1.A16.25monomerHHblitsX-ray1.63Å0.260.45Reticuline oxidase; Berberine bridge-forming enzyme
4uhw.1.A11.88homo-dimerHHblitsX-ray2.60Å0.260.45ALDEHYDE OXIDASE
5epg.1.A11.88homo-dimerHHblitsX-ray3.39Å0.260.45Aldehyde oxidase
3fw8.1.A14.91monomerHHblitsX-ray1.50Å0.260.46Reticuline oxidase
4ec3.1.A16.25monomerHHblitsX-ray2.65Å0.260.45Reticuline oxidase
2wdw.1.A13.13homo-dimerHHblitsX-ray3.21Å0.260.45PUTATIVE HEXOSE OXIDASE
5awv.1.C13.13homo-tetramerHHblitsX-ray1.93Å0.260.45Putative hexose oxidase
3zyv.1.A11.32homo-dimerHHblitsX-ray2.55Å0.260.45AOX3
2ipi.1.A14.38monomerHHblitsX-ray1.65Å0.250.45Aclacinomycin oxidoreductase (AknOx)
5i1v.1.A13.13homo-dimerHHblitsX-ray1.84Å0.250.45CrmK
2y3r.1.A13.75homo-dimerHHblitsX-ray1.79Å0.250.45TAML
1n62.1.C16.67hetero-oligomerHHblitsX-ray1.09Å0.280.42Carbon monoxide dehydrogenase medium chain
1zxi.1.C15.44hetero-oligomerHHblitsX-ray1.70Å0.280.42Carbon monoxide dehydrogenase medium chain
1ffu.1.C15.44hetero-oligomerHHblitsX-ray2.35Å0.280.42CUTM, FLAVOPROTEIN OF CARBON MONOXIDE DEHYDROGENASE
1ffv.1.C15.44hetero-oligomerHHblitsX-ray2.25Å0.280.42CUTM, FLAVOPROTEIN OF CARBON MONOXIDE DEHYDROGENASE
4zoh.1.B12.24hetero-oligomerHHblitsX-ray2.20Å0.270.42Putative oxidoreductase FAD-binding subunit
5mxj.1.A14.60homo-octamerHHblitsX-ray2.80Å0.270.39Vanillyl-alcohol oxidase
1qlt.1.A14.60homo-octamerHHblitsX-ray2.20Å0.270.39VANILLYL-ALCOHOL OXIDASE
1w1l.1.A13.87homo-dimerHHblitsX-ray2.70Å0.270.39VANILLYL-ALCOHOL OXIDASE
1e0y.1.A13.87homo-dimerHHblitsX-ray2.75Å0.270.39VANILLYL-ALCOHOL OXIDASE
1f0x.1.A10.08monomerHHblitsX-ray1.90Å0.240.37D-LACTATE DEHYDROGENASE
4g3t.1.A17.95monomerHHblitsX-ray2.35Å0.290.33oxidoreductase DprE1
2yvs.1.A9.00homo-dimerHHblitsX-ray2.00Å0.230.28Glycolate oxidase subunit GlcE
2yvs.1.B9.00homo-dimerHHblitsX-ray2.00Å0.230.28Glycolate oxidase subunit GlcE
3b9j.1.B9.76hetero-oligomerHHblitsX-ray2.30Å0.270.23xanthine oxidase
4hti.1.A15.00monomerHHblitsX-ray1.95Å0.280.23Receptor-type tyrosine-protein phosphatase N2
4htj.1.A15.00monomerHHblitsX-ray2.01Å0.280.23Receptor-type tyrosine-protein phosphatase N2
2ze3.1.A16.33homo-dimerHHblitsX-ray1.65Å0.290.14DFA0005
1m1b.1.A16.33homo-tetramerHHblitsX-ray2.25Å0.280.14PHOSPHOENOLPYRUVATE PHOSPHOMUTASE
1s2v.1.A16.33homo-tetramerHHblitsX-ray2.10Å0.280.14Phosphoenolpyruvate phosphomutase
1s2w.1.A16.33monomerHHblitsX-ray1.69Å0.280.14Phosphoenolpyruvate phosphomutase
2hjp.1.A16.33homo-tetramerHHblitsX-ray1.90Å0.280.14Phosphonopyruvate hydrolase
3m0k.1.A14.29homo-tetramerHHblitsX-ray1.65Å0.280.14Oxaloacetate acetylhydrolase
1s2u.1.A16.33homo-tetramerHHblitsX-ray2.00Å0.280.14Phosphoenolpyruvate phosphomutase
5unc.1.A12.24homo-tetramerHHblitsX-ray1.71Å0.270.14PHOSPHOENOLPYRUVATE PHOSPHOMUTASE
4iqd.1.A10.20homo-dimerHHblitsX-ray2.00Å0.260.14Carboxyvinyl-carboxyphosphonate phosphorylmutase
4iqe.1.B10.20homo-dimerHHblitsX-ray2.50Å0.260.14Carboxyvinyl-carboxyphosphonate phosphorylmutase
1wn2.1.A20.51homo-dimerHHblitsX-ray1.20Å0.280.11Peptidyl-tRNA hydrolase
2d3k.1.A20.51homo-dimerHHblitsX-ray1.90Å0.280.11Peptidyl-tRNA hydrolase
1xty.1.A17.95homo-dimerHHblitsX-ray1.80Å0.270.11Peptidyl-tRNA hydrolase
2zv3.1.A12.82homo-dimerHHblitsX-ray2.10Å0.260.11Peptidyl-tRNA hydrolase
2zv3.3.B12.82homo-dimerHHblitsX-ray2.10Å0.260.11Peptidyl-tRNA hydrolase
2zv3.4.A12.82homo-dimerHHblitsX-ray2.10Å0.260.11Peptidyl-tRNA hydrolase
2zv3.4.B12.82homo-dimerHHblitsX-ray2.10Å0.260.11Peptidyl-tRNA hydrolase
4ohq.1.A13.16homo-dimerHHblitsX-ray2.15Å0.280.11Triosephosphate isomerase, chloroplastic
1dkw.1.A10.53homo-dimerHHblitsX-ray2.65Å0.270.11TRIOSEPHOSPHATE ISOMERASE
2vei.1.A10.53homo-trimerHHblitsX-ray1.89Å0.270.11GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE
2vei.1.B10.53homo-trimerHHblitsX-ray1.89Å0.270.11GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE
2vei.1.C10.53homo-trimerHHblitsX-ray1.89Å0.270.11GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE
2x16.1.A10.53monomerHHblitsX-ray2.13Å0.270.11TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL
4pc8.1.A10.53monomerHHblitsX-ray1.55Å0.270.11Ma21-TIM
1rlk.1.A18.42monomerHHblitsX-ray1.95Å0.270.11Hypothetical protein Ta0108
1ney.1.A10.53homo-dimerHHblitsX-ray1.20Å0.270.11triosephosphate isomerase
1nf0.1.A10.53homo-dimerHHblitsX-ray1.60Å0.270.11triosephosphate isomerase
4unl.1.A5.26homo-dimerHHblitsX-ray1.50Å0.270.11TRIOSEPHOSPHATE ISOMERASE
2vom.1.A5.26homo-dimerHHblitsX-ray1.85Å0.270.11TRIOSEPHOSPHATE ISOMERASE
4pod.1.A5.26homo-dimerHHblitsX-ray1.99Å0.270.11Triosephosphate isomerase
4pod.1.B5.26homo-dimerHHblitsX-ray1.99Å0.270.11Triosephosphate isomerase
1wyi.1.A5.26homo-tetramerHHblitsX-ray2.20Å0.270.11Triosephosphate isomerase
1wyi.1.B5.26homo-tetramerHHblitsX-ray2.20Å0.270.11Triosephosphate isomerase
1hti.1.A5.26homo-dimerHHblitsX-ray2.80Å0.270.11TRIOSEPHOSPHATE ISOMERASE
1hti.1.B5.26homo-dimerHHblitsX-ray2.80Å0.270.11TRIOSEPHOSPHATE ISOMERASE
4br1.1.A5.26homo-dimerHHblitsX-ray1.90Å0.270.11TRIOSEPHOSPHATE ISOMERASE
4unk.1.A5.26homo-dimerHHblitsX-ray2.00Å0.270.11TRIOSEPHOSPHATE ISOMERASE
1tim.1.A5.26homo-dimerHHblitsX-ray2.50Å0.270.11TRIOSEPHOSPHATE ISOMERASE
1tim.1.B5.26homo-dimerHHblitsX-ray2.50Å0.270.11TRIOSEPHOSPHATE ISOMERASE
1q7s.1.A21.05monomerHHblitsX-ray2.00Å0.270.11bit1
1q7s.2.A21.05monomerHHblitsX-ray2.00Å0.270.11bit1
1tph.1.A5.26homo-dimerHHblitsX-ray1.80Å0.270.11TRIOSEPHOSPHATE ISOMERASE
8tim.1.A5.26homo-dimerHHblitsX-ray2.50Å0.270.11TRIOSE PHOSPHATE ISOMERASE
8tim.1.B5.26homo-dimerHHblitsX-ray2.50Å0.270.11TRIOSE PHOSPHATE ISOMERASE
1sw3.1.A5.26homo-dimerHHblitsX-ray2.03Å0.260.11Triosephosphate isomerase
1ssg.1.A2.63homo-dimerHHblitsX-ray2.90Å0.260.11Triosephosphate isomerase
1su5.1.A2.63homo-dimerHHblitsX-ray2.70Å0.250.11Triosephosphate isomerase
3erj.1.A18.42homo-dimerHHblitsX-ray1.80Å0.250.11Peptidyl-tRNA hydrolase
3erj.1.B18.42homo-dimerHHblitsX-ray1.80Å0.250.11Peptidyl-tRNA hydrolase
1rzw.1.A18.42monomerHHblitsNMRNA0.250.11Protein AF2095(GR4)
2lnd.1.A18.75monomerHHblitsNMRNA0.310.09DE NOVO DESIGNED PROTEIN, PFK fold
2ki0.1.A12.12monomerHHblitsNMRNA0.260.09DS119