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 |
|---|---|---|---|
| 2eq7 | FAD | Dihydrolipoyl dehydrogenase |
| PDB ID | HET | Uniprot Name | EC Number | Cavity Similarity |
Align |
|---|---|---|---|---|---|
| 2eq7 | FAD | Dihydrolipoyl dehydrogenase | / | 1.000 | |
| 1jeh | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.500 | |
| 1zmc | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.484 | |
| 1zmd | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.483 | |
| 4jq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.480 | |
| 3urh | FAD | Dihydrolipoyl dehydrogenase | / | 0.479 | |
| 3lad | FAD | Dihydrolipoyl dehydrogenase | / | 0.468 | |
| 1zk7 | FAD | Mercuric reductase | 1.16.1.1 | 0.457 | |
| 4jdr | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.456 | |
| 1geu | FAD | Glutathione reductase | 1.8.1.7 | 0.455 | |
| 1lpf | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.449 | |
| 1lvl | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.446 |