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 |
|---|---|---|---|
| 1lpf | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 |
| PDB ID | HET | Uniprot Name | EC Number | Cavity Similarity |
Align |
|---|---|---|---|---|---|
| 1lpf | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 1.000 | |
| 3lad | FAD | Dihydrolipoyl dehydrogenase | / | 0.609 | |
| 2qae | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.573 | |
| 2f5z | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.553 | |
| 4jdr | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.549 | |
| 2eq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.533 | |
| 4jq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.528 | |
| 3rnm | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.526 | |
| 1jeh | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.521 | |
| 2yqu | FAD | Dihydrolipoyl dehydrogenase | / | 0.516 | |
| 1zy8 | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.511 | |
| 1zmc | FAD | Dihydrolipoyl dehydrogenase, mitochondrial | 1.8.1.4 | 0.509 | |
| 3urh | FAD | Dihydrolipoyl dehydrogenase | / | 0.497 | |
| 1zk7 | FAD | Mercuric reductase | 1.16.1.1 | 0.494 | |
| 1zx9 | FAD | Mercuric reductase | 1.16.1.1 | 0.488 | |
| 4m52 | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.485 | |
| 3cgb | FAD | Coenzyme A disulfide reductase | / | 0.454 | |
| 2r9z | FAD | Glutathione amide reductase | / | 0.448 | |
| 2a8x | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.444 | |
| 1k4q | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.443 | |
| 1xdi | FAD | NAD(P)H dehydrogenase (quinone) | / | 0.440 | |
| 3cgc | FAD | Coenzyme A disulfide reductase | / | 0.440 |