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 |
|---|---|---|---|
| 2eq9 | FAD | Dihydrolipoyl dehydrogenase |
| PDB ID | HET | Uniprot Name | EC Number | Cavity Similarity |
Align |
|---|---|---|---|---|---|
| 2eq9 | FAD | Dihydrolipoyl dehydrogenase | / | 1.000 | |
| 2eq6 | FAD | Dihydrolipoyl dehydrogenase | / | 0.517 | |
| 4jq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.507 | |
| 2f5z | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.501 | |
| 1zy8 | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.497 | |
| 2qae | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.489 | |
| 1zk7 | FAD | Mercuric reductase | 1.16.1.1 | 0.482 | |
| 4jdr | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.479 | |
| 3rnm | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.460 | |
| 2yqu | FAD | Dihydrolipoyl dehydrogenase | / | 0.456 | |
| 1zx9 | FAD | Mercuric reductase | 1.16.1.1 | 0.453 | |
| 1zmc | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.448 | |
| 3lad | FAD | Dihydrolipoyl dehydrogenase | / | 0.447 | |
| 1jeh | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.440 |