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 |
|---|---|---|---|
| 1zmd | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 |
| PDB ID | HET | Uniprot Name | EC Number | Cavity Similarity |
Align |
|---|---|---|---|---|---|
| 1zmd | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 1.000 | |
| 1zmc | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.605 | |
| 2eq7 | FAD | Dihydrolipoyl dehydrogenase | / | 0.577 | |
| 1lvl | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.544 | |
| 3lad | FAD | Dihydrolipoyl dehydrogenase | / | 0.543 | |
| 1lpf | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.541 | |
| 1jeh | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.526 | |
| 1geu | FAD | Glutathione reductase | 1.8.1.7 | 0.525 | |
| 1zk7 | FAD | Mercuric reductase | 1.16.1.1 | 0.514 | |
| 3urh | FAD | Dihydrolipoyl dehydrogenase | / | 0.507 | |
| 2eq8 | FAD | Dihydrolipoyl dehydrogenase | / | 0.505 | |
| 1onf | FAD | Glutathione reductase | 1.8.1.7 | 0.501 | |
| 2gh5 | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.496 | |
| 2rab | FAD | Glutathione amide reductase | / | 0.495 | |
| 2r9z | FAD | Glutathione amide reductase | / | 0.494 | |
| 4jdr | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.492 | |
| 1grb | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.482 | |
| 2zzc | FAD | Thioredoxin reductase 1, cytoplasmic | 1.8.1.9 | 0.481 | |
| 1ger | FAD | Glutathione reductase | 1.8.1.7 | 0.465 | |
| 1nhq | FAD | NADH peroxidase | 1.11.1.1 | 0.455 | |
| 3dgh | FAD | Thioredoxin reductase 1, mitochondrial | 1.8.1.9 | 0.454 | |
| 1get | FAD | Glutathione reductase | 1.8.1.7 | 0.453 | |
| 3djg | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.453 |