Research workbench
AlphaFold monomer V2.0 prediction for retinol-binding protein 4 (P06912)
Analyse AlphaFold monomer V2.0 prediction for retinol-binding protein 4 (P06912) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P06912
- Type
- protein
- Length
- 201 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x299fdAcA3f0bf08962C6B6e8201Eb8953a8483fB
- Molecule
- Retinol-binding protein 4
- UniProt
- P06912
- Pockets
- 2 · best druggability 0.81
Structure
1 distinct chain · 17% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinol-binding protein 4 | protein | 201 | 17% helix, 42% strand | P06912 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.81 | 0.94 | 29 | empty |
| 2 | 67 | 0.31 | 0.74 | 13 | empty |
Modifications
Observed in the structure: 3 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 P06912
- Elsewhere: UniProt P06912 · AlphaFold DB P06912
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