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 |
|---|---|---|---|
| 4la1 | FAD | Thioredoxin glutathione reductase |
| PDB ID | HET | Uniprot Name | EC Number | Cavity Similarity |
Align |
|---|---|---|---|---|---|
| 4la1 | FAD | Thioredoxin glutathione reductase | / | 1.000 | |
| 4dna | FAD | Probable glutathione reductase | / | 0.588 | |
| 3dgz | FAD | Thioredoxin reductase 2, mitochondrial | 1.8.1.9 | 0.573 | |
| 1fec | FAD | Trypanothione reductase | 1.8.1.12 | 0.572 | |
| 1grh | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.570 | |
| 2hqm | FAD | Glutathione reductase | 1.8.1.7 | 0.565 | |
| 4kpr | FAD | Thioredoxin reductase 1, cytoplasmic | 1.8.1.9 | 0.559 | |
| 1tyt | FAD | Trypanothione reductase | 1.8.1.12 | 0.554 | |
| 2jk6 | FAD | Trypanothione reductase | / | 0.550 | |
| 4j56 | FAD | Thioredoxin reductase 2 | 1.8.1.9 | 0.544 | |
| 1k4q | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.539 | |
| 4gr1 | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.507 | |
| 2wba | FAD | Trypanothione reductase | 1.8.1.12 | 0.504 | |
| 1gxf | FAD | Trypanothione reductase | 1.8.1.12 | 0.499 | |
| 2v6o | FAD | Thioredoxin glutathione reductase | / | 0.499 | |
| 2x8h | FAD | Thioredoxin glutathione reductase | / | 0.496 | |
| 1bzl | FAD | Trypanothione reductase | 1.8.1.12 | 0.475 | |
| 4nev | FAD | Trypanothione reductase | / | 0.472 | |
| 2j3n | FAD | Thioredoxin reductase 1, cytoplasmic | 1.8.1.9 | 0.461 | |
| 2qae | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.459 | |
| 2eq9 | FAD | Dihydrolipoyl dehydrogenase | / | 0.453 | |
| 1dnc | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.450 | |
| 3grs | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.440 |