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 |
|---|---|---|---|
| 2qae | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 |
| PDB ID | HET | Uniprot Name | EC Number | Cavity Similarity |
Align |
|---|---|---|---|---|---|
| 2qae | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 1.000 | |
| 2f5z | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.585 | |
| 3lad | FAD | Dihydrolipoyl dehydrogenase | / | 0.584 | |
| 2yqu | FAD | Dihydrolipoyl dehydrogenase | / | 0.567 | |
| 2eq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.561 | |
| 3rnm | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.556 | |
| 1jeh | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.536 | |
| 1lpf | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.532 | |
| 1zy8 | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.521 | |
| 4jq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.520 | |
| 1zmc | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.501 | |
| 2eq6 | FAD | Dihydrolipoyl dehydrogenase | / | 0.494 | |
| 3urh | FAD | Dihydrolipoyl dehydrogenase | / | 0.494 | |
| 1zx9 | FAD | Mercuric reductase | 1.16.1.1 | 0.479 | |
| 1zk7 | FAD | Mercuric reductase | 1.16.1.1 | 0.477 | |
| 4jdr | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.467 | |
| 4m52 | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.463 | |
| 3cgc | FAD | Coenzyme A disulfide reductase | / | 0.451 | |
| 3cgb | FAD | Coenzyme A disulfide reductase | / | 0.450 |