Binding Sites are compared using Shaper.
For more information, please see the following publication:
Desaphy J. et al. Comparison and Druggability Prediction of protein-Ligand Binding sites from pharmacophore-annotated cavity shapes J. Chem. Inf. Model., 2012, 52(8), pp2287-2299
Binding Sites are considered as similar when the similarity value is greater than 0.44
PDB ID | HET | Uniprot Name | EC Number |
---|---|---|---|
3icp | NAD | NAD-dependent epimerase/dehydratase |
PDB ID | HET | Uniprot Name | EC Number | Binding Site Similarity |
Align |
---|---|---|---|---|---|
3icp | NAD | NAD-dependent epimerase/dehydratase | / | 1.000 | |
3ko8 | NAD | NAD-dependent epimerase/dehydratase | / | 0.788 | |
3ehe | NAD | UDP-glucose 4-epimerase (GalE-1) | / | 0.589 | |
3ruf | NAD | UDP-N-acetylglucosamine 4-epimerase | / | 0.496 | |
3ru7 | NAD | UDP-N-acetylglucosamine 4-epimerase | / | 0.491 | |
3ru9 | NAD | UDP-N-acetylglucosamine 4-epimerase | / | 0.491 | |
3rud | NAD | UDP-N-acetylglucosamine 4-epimerase | / | 0.490 | |
3rue | NAD | UDP-N-acetylglucosamine 4-epimerase | / | 0.484 | |
2q1w | NAD | Putative nucleotide sugar epimerase/ dehydratase | / | 0.480 | |
3lu1 | NAD | UDP-N-acetylglucosamine 4-epimerase | / | 0.475 | |
2hun | NAD | 336aa long hypothetical dTDP-glucose 4,6-dehydratase | / | 0.473 | |
4gll | NAD | UDP-glucuronic acid decarboxylase 1 | 4.1.1.35 | 0.471 | |
3rua | NAD | UDP-N-acetylglucosamine 4-epimerase | / | 0.467 | |
2p5u | NAD | UDP-glucose 4-epimerase | / | 0.466 | |
2c20 | NAD | UDP-glucose 4-epimerase | / | 0.455 | |
3ruc | NAD | UDP-N-acetylglucosamine 4-epimerase | / | 0.455 | |
2pzj | NAD | Putative nucleotide sugar epimerase/ dehydratase | / | 0.454 | |
4egb | NAD | dTDP-glucose 4,6-dehydratase | / | 0.451 | |
1g1a | NAD | dTDP-glucose 4,6-dehydratase | / | 0.450 | |
4twr | NAD | NAD binding site:NAD-dependent epimerase/dehydratase:UDP-glucose 4-epimerase | / | 0.448 | |
1bxk | NAD | dTDP-glucose 4,6-dehydratase 2 | / | 0.445 | |
3sxp | NAD | ADP-L-glycero-D-mannoheptose-6-epimerase | / | 0.441 |