Cavities 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
| PDB ID | HET | Uniprot Name | EC Number |
|---|---|---|---|
| 1bzf | TMQ | Dihydrofolate reductase | 1.5.1.3 |
| PDB ID | HET | Uniprot Name | EC Number | Cavity Similarity |
Align |
|---|---|---|---|---|---|
| 1bzf | TMQ | Dihydrofolate reductase | 1.5.1.3 | 1.000 | |
| 1dis | BDM | Dihydrofolate reductase | 1.5.1.3 | 0.494 | |
| 1diu | BDM | Dihydrofolate reductase | 1.5.1.3 | 0.492 | |
| 1dds | MTX | Dihydrofolate reductase | 1.5.1.3 | 0.469 | |
| 2h2q | NAP | Bifunctional dihydrofolate reductase-thymidylate synthase | 1.5.1.3 | 0.460 | |
| 1dhf | FOL | Dihydrofolate reductase | 1.5.1.3 | 0.459 | |
| 1re7 | FOL | Dihydrofolate reductase | 1.5.1.3 | 0.453 | |
| 2cig | 1DG | Dihydrofolate reductase | 1.5.1.3 | 0.449 | |
| 1rb3 | MTX | Dihydrofolate reductase | 1.5.1.3 | 0.448 | |
| 4cd2 | FOL | Dihydrofolate reductase | 1.5.1.3 | 0.447 | |
| 1ddr | MTX | Dihydrofolate reductase | 1.5.1.3 | 0.446 | |
| 2drc | MTX | Dihydrofolate reductase | 1.5.1.3 | 0.443 | |
| 1ao8 | MTX | Dihydrofolate reductase | 1.5.1.3 | 0.442 | |
| 2dhf | DZF | Dihydrofolate reductase | 1.5.1.3 | 0.442 | |
| 3irm | 1CY | Bifunctional dihydrofolate reductase-thymidylate synthase | 1.5.1.3 | 0.442 | |
| 3kjs | NAP | Bifunctional dihydrofolate reductase-thymidylate synthase | / | 0.442 | |
| 1ia3 | TQ5 | Dihydrofolate reductase | 1.5.1.3 | 0.441 | |
| 1dr3 | TAP | Dihydrofolate reductase | 1.5.1.3 | 0.440 | |
| 1dra | MTX | Dihydrofolate reductase | 1.5.1.3 | 0.440 | |
| 3hbb | NAP | Bifunctional dihydrofolate reductase-thymidylate synthase | 1.5.1.3 | 0.440 |