Research workbench
AlphaFold monomer V2.0 prediction for transmembrane protein 267 (Q8VDR5)
Analyse AlphaFold monomer V2.0 prediction for transmembrane protein 267 (Q8VDR5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8VDR5
- Type
- protein
- Length
- 215 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- Transmembrane protein 267
- UniProt
- Q8VDR5
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transmembrane protein 267 | protein | 215 | 69% helix, 2% strand | Q8VDR5 |
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 | 244 | 0.65 | 0.83 | 32 | empty |
| 2 | 193 | 0.55 | 0.79 | 25 | empty |
| 3 | 58 | 0.31 | 0.76 | 12 | empty |
| 4 | 53 | 0.30 | 0.76 | 12 | empty |
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 Q8VDR5
- Elsewhere: UniProt Q8VDR5 · AlphaFold DB Q8VDR5
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