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 |
|---|---|---|---|
| 3urh | FAD | Dihydrolipoyl dehydrogenase |
| PDB ID | HET | Uniprot Name | EC Number | Cavity Similarity |
Align |
|---|---|---|---|---|---|
| 3urh | FAD | Dihydrolipoyl dehydrogenase | / | 1.000 | |
| 2qae | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.561 | |
| 2yqu | FAD | Dihydrolipoyl dehydrogenase | / | 0.561 | |
| 1jeh | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.552 | |
| 2f5z | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.536 | |
| 2eq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.531 | |
| 3lad | FAD | Dihydrolipoyl dehydrogenase | / | 0.514 | |
| 1zy8 | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.503 | |
| 4jq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.503 | |
| 1zk7 | FAD | Mercuric reductase | 1.16.1.1 | 0.500 | |
| 1zmc | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.496 | |
| 1lpf | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.492 | |
| 1zx9 | FAD | Mercuric reductase | 1.16.1.1 | 0.488 | |
| 4jdr | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.488 | |
| 3cgc | FAD | Coenzyme A disulfide reductase | / | 0.450 | |
| 4m52 | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.447 | |
| 3ic9 | FAD | Putative dihydrolipoamide dehydrogenase | / | 0.443 | |
| 2r9z | FAD | Glutathione amide reductase | / | 0.442 |