Research workbench
AlphaFold monomer V2.0 prediction for oligopeptide transporter 4 (Q9FME8)
Analyse AlphaFold monomer V2.0 prediction for oligopeptide transporter 4 (Q9FME8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9FME8
- Type
- protein
- Length
- 729 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x05AE9FA8dE2A69C3b73cE5754D771B45C078eBf2
- Molecule
- Oligopeptide transporter 4
- UniProt
- Q9FME8
- Pockets
- 8 · best druggability 0.87
Structure
1 distinct chain · 65% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oligopeptide transporter 4 | protein | 729 | 65% helix, 2% strand | Q9FME8 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1177 | 0.87 | 0.89 | 121 | empty |
| 2 | 217 | 0.53 | 0.77 | 28 | empty |
| 3 | 132 | 0.44 | 0.77 | 19 | empty |
| 4 | 92 | 0.44 | 0.79 | 15 | empty |
| 5 | 93 | 0.41 | 0.77 | 16 | 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 Q9FME8
- Elsewhere: UniProt Q9FME8 · AlphaFold DB Q9FME8
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