Research workbench
AlphaFold monomer V2.0 prediction for oxygen-regulated protein 1 (P56715)
Analyse AlphaFold monomer V2.0 prediction for oxygen-regulated protein 1 (P56715) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P56715
- Type
- protein
- Length
- 2,156 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Oxygen-regulated protein 1
- UniProt
- P56715
- Pockets
- 4 · best druggability 0.59
Structure
1 distinct chain · 6% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxygen-regulated protein 1 | protein | 2156 | 6% helix, 3% strand | P56715 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 338 | 0.59 | 0.77 | 43 | empty |
| 2 | 62 | 0.38 | 0.79 | 13 | empty |
| 3 | 66 | 0.31 | 0.75 | 12 | empty |
| 4 | 52 | 0.26 | 0.72 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P56715
- Elsewhere: UniProt P56715 · AlphaFold DB P56715
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