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 |
|---|---|---|---|
| 3ict | FAD | Coenzyme A disulfide reductase |
| PDB ID | HET | Uniprot Name | EC Number | Cavity Similarity |
Align |
|---|---|---|---|---|---|
| 3ict | FAD | Coenzyme A disulfide reductase | / | 1.000 | |
| 3icr | FAD | Coenzyme A disulfide reductase | / | 0.567 | |
| 3nta | FAD | FAD-dependent pyridine nucleotide-disulphide oxidoreductase | / | 0.538 | |
| 3ics | FAD | Coenzyme A disulfide reductase | / | 0.527 | |
| 3ntd | FAD | FAD-dependent pyridine nucleotide-disulphide oxidoreductase | / | 0.525 | |
| 4ocg | FAD | FAD-dependent pyridine nucleotide-disulphide oxidoreductase | / | 0.501 | |
| 2eq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.500 | |
| 3cgb | FAD | Coenzyme A disulfide reductase | / | 0.484 | |
| 3cgc | FAD | Coenzyme A disulfide reductase | / | 0.473 | |
| 1zy8 | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.464 | |
| 2eq6 | FAD | Dihydrolipoyl dehydrogenase | / | 0.458 | |
| 3rnm | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.452 | |
| 2qae | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.448 | |
| 2yqu | FAD | Dihydrolipoyl dehydrogenase | / | 0.447 | |
| 4eqw | FAD | Coenzyme A disulfide reductase | / | 0.446 | |
| 4eqs | FAD | Coenzyme A disulfide reductase | / | 0.444 | |
| 4jq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.441 |