Research workbench
AlphaFold monomer V2.0 prediction for transmembrane protein 104 (Q5RCV1)
Analyse AlphaFold monomer V2.0 prediction for transmembrane protein 104 (Q5RCV1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5RCV1
- Type
- protein
- Length
- 496 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x01d27036D0b2F2b48590ff9F414E8DC840974276
- Molecule
- Transmembrane protein 104
- UniProt
- Q5RCV1
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 69% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transmembrane protein 104 | protein | 496 | 69% helix, 1% strand | Q5RCV1 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 995 | 0.78 | 0.80 | 67 | empty |
| 2 | 487 | 0.66 | 0.78 | 53 | empty |
| 3 | 54 | 0.47 | 0.85 | 13 | empty |
| 4 | 108 | 0.40 | 0.75 | 20 | 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 Q5RCV1
- Elsewhere: UniProt Q5RCV1 · AlphaFold DB Q5RCV1
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