Research workbench
AlphaFold monomer V2.0 prediction for oxysterol-binding protein 1 (P16258)
Analyse AlphaFold monomer V2.0 prediction for oxysterol-binding protein 1 (P16258) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P16258
- Type
- protein
- Length
- 809 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- Oxysterol-binding protein 1
- UniProt
- P16258
- Pockets
- 10 · best druggability 0.83
Structure
1 distinct chain · 33% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxysterol-binding protein 1 | protein | 809 | 33% helix, 20% strand | P16258 |
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 238 | 0.83 | 0.96 | 34 | empty |
| 2 | 438 | 0.67 | 0.79 | 39 | empty |
| 3 | 260 | 0.54 | 0.77 | 36 | empty |
| 4 | 144 | 0.49 | 0.78 | 26 | empty |
| 5 | 105 | 0.49 | 0.81 | 18 | 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 P16258
- Elsewhere: UniProt P16258 · AlphaFold DB P16258
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