Binding Modes are compared using Grim.
For more information, please see the following publication:
Desaphy J. et al. Encoding Protein-Ligand Interaction Patterns in Fingerprints and Graphs J. Chem. Inf. Model., 2013, 53 (3), pp 623-637
Binding modes are considered as similar when the similarity value is greater than 0.65
| PDB ID | HET | Uniprot Name | EC Number |
|---|---|---|---|
| 3w4y | FAD | Mitochondrial FAD-linked sulfhydryl oxidase ERV1 | 1.8.3.2 |
| PDB ID | HET | Uniprot Name | EC Number | Binding Mode Similarity |
Align |
|---|---|---|---|---|---|
| 3w4y | FAD | Mitochondrial FAD-linked sulfhydryl oxidase ERV1 | 1.8.3.2 | 1.484 | |
| 3u2l | FAD | FAD-linked sulfhydryl oxidase ALR | 1.8.3.2 | 1.142 | |
| 4e0i | FAD | Mitochondrial FAD-linked sulfhydryl oxidase ERV1 | 1.8.3.2 | 1.140 | |
| 4e0h | FAD | Mitochondrial FAD-linked sulfhydryl oxidase ERV1 | 1.8.3.2 | 1.131 | |
| 3mbg | FAD | FAD-linked sulfhydryl oxidase ALR | 1.8.3.2 | 1.118 | |
| 1oqc | FAD | FAD-linked sulfhydryl oxidase ALR | 1.8.3.2 | 1.070 | |
| 3u5s | FAD | FAD-linked sulfhydryl oxidase ALR | 1.8.3.2 | 1.051 | |
| 3tk0 | FAD | FAD-linked sulfhydryl oxidase ALR | 1.8.3.2 | 1.049 | |
| 4ldk | FAD | FAD-linked sulfhydryl oxidase ALR | 1.8.3.2 | 1.027 | |
| 1jr8 | FAD | FAD-linked sulfhydryl oxidase ERV2 | 1.8.3.2 | 0.989 | |
| 3r7c | FAD | FAD-linked sulfhydryl oxidase ALR | 1.8.3.2 | 0.965 | |
| 3u2m | FAD | FAD-linked sulfhydryl oxidase ALR | 1.8.3.2 | 0.962 | |
| 2hj3 | FAD | FAD-linked sulfhydryl oxidase ERV1 | / | 0.924 | |
| 3t58 | FAD | Sulfhydryl oxidase 1 | 1.8.3.2 | 0.885 | |
| 1jra | FAD | FAD-linked sulfhydryl oxidase ERV2 | 1.8.3.2 | 0.854 | |
| 3lli | FAD | Sulfhydryl oxidase 1 | 1.8.3.2 | 0.854 | |
| 3llk | FAD | Sulfhydryl oxidase 1 | 1.8.3.2 | 0.826 | |
| 3gwl | FAD | FAD-linked sulfhydryl oxidase | 1.8.3.2 | 0.802 | |
| 3t59 | FAD | Sulfhydryl oxidase 1 | 1.8.3.2 | 0.773 | |
| 4p2l | FAD | Sulfhydryl oxidase 1 | 1.8.3.2 | 0.757 | |
| 3ust | FAD | AcMNPV orf92 | / | 0.748 | |
| 3qzy | FAD | FAD-linked sulfhydryl oxidase | / | 0.746 | |
| 3gwn | FAD | Probable FAD-linked sulfhydryl oxidase R596 | 1.8.3.2 | 0.709 | |
| 4opg | FDA | Conserved Archaeal protein | / | 0.683 | |
| 4opi | FDA | Conserved Archaeal protein | / | 0.681 | |
| 4opl | FDA | Conserved Archaeal protein | / | 0.681 | |
| 4opt | FDA | Conserved Archaeal protein | / | 0.681 | |
| 4opu | FDA | Conserved Archaeal protein | / | 0.681 | |
| 1rp4 | FAD | Endoplasmic oxidoreductin-1 | 1.8.4 | 0.676 | |
| 3atq | FDA | Conserved Archaeal protein | / | 0.668 | |
| 5j3w | FMN | Sensory box protein | / | 0.667 | |
| 3atr | FDA | Conserved Archaeal protein | / | 0.666 | |
| 1ryi | FAD | Glycine oxidase | 1.4.3.19 | 0.665 | |
| 3td7 | FAD | Probable FAD-linked sulfhydryl oxidase R596 | 1.8.3.2 | 0.661 | |
| 3ic9 | FAD | Putative dihydrolipoamide dehydrogenase | / | 0.660 | |
| 2gqw | FAD | Ferredoxin reductase | / | 0.658 | |
| 4h4r | FAD | Biphenyl dioxygenase ferredoxin reductase subunit | / | 0.658 | |
| 4h4t | FAD | Biphenyl dioxygenase ferredoxin reductase subunit | / | 0.658 | |
| 4h4v | FAD | Biphenyl dioxygenase ferredoxin reductase subunit | / | 0.658 | |
| 4h4x | FAD | Biphenyl dioxygenase ferredoxin reductase subunit | / | 0.658 | |
| 1krh | FAD | Benzoate 1,2-dioxygenase electron transfer component | 1.18.1.3 | 0.657 | |
| 1ps9 | FAD | 2,4-dienoyl-CoA reductase | 1.3.1.34 | 0.657 | |
| 3ept | FDA | Putative FAD-monooxygenase | / | 0.652 | |
| 4ees | FMN | Phototropin-2 | 2.7.11.1 | 0.651 | |
| 4hj4 | FMN | LOV protein | / | 0.651 | |
| 3sqx | ANP | ATP-dependent RNA helicase MSS116, mitochondrial | 3.6.4.13 | 0.650 | |
| 4jnq | FDA | Thioredoxin reductase | / | 0.650 |