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 |
---|---|---|---|
1gxf | FAD | Trypanothione reductase | 1.8.1.12 |
PDB ID | HET | Uniprot Name | EC Number | Cavity Similarity |
Align |
---|---|---|---|---|---|
1gxf | FAD | Trypanothione reductase | 1.8.1.12 | 1.000 | |
1bzl | FAD | Trypanothione reductase | 1.8.1.12 | 0.589 | |
2jk6 | FAD | Trypanothione reductase | / | 0.582 | |
4dna | FAD | Probable glutathione reductase | / | 0.581 | |
1fec | FAD | Trypanothione reductase | 1.8.1.12 | 0.578 | |
2hqm | FAD | Glutathione reductase | 1.8.1.7 | 0.567 | |
2wba | FAD | Trypanothione reductase | 1.8.1.12 | 0.562 | |
1tyt | FAD | Trypanothione reductase | 1.8.1.12 | 0.559 | |
1grh | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.541 | |
1k4q | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.540 | |
4j56 | FAD | Thioredoxin reductase 2 | 1.8.1.9 | 0.523 | |
1feb | FAD | Trypanothione reductase | 1.8.1.12 | 0.519 | |
4la1 | FAD | Thioredoxin glutathione reductase | / | 0.498 | |
3grs | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.478 | |
4gr1 | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.471 | |
4fx9 | FAD | Coenzyme A disulfide reductase | 1.8.1.14 | 0.460 | |
3nta | FAD | FAD-dependent pyridine nucleotide-disulphide oxidoreductase | / | 0.451 | |
4j57 | FAD | Thioredoxin reductase 2 | 1.8.1.9 | 0.448 | |
2tpr | FAD | Trypanothione reductase | 1.8.1.12 | 0.445 | |
2qae | FAD | Dihydrolipoyl dehydrogenase | 1.8.1.4 | 0.442 | |
1dnc | FAD | Glutathione reductase, mitochondrial | 1.8.1.7 | 0.441 | |
3ntd | FAD | FAD-dependent pyridine nucleotide-disulphide oxidoreductase | / | 0.441 |