Research workbench
AlphaFold monomer V2.0 prediction for transmembrane protein 94 (Q12767)
Analyse AlphaFold monomer V2.0 prediction for transmembrane protein 94 (Q12767) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12767
- Type
- protein
- Length
- 1,356 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBa07a45B8DC60898f701d03c6ae0Ec6dD18010B2
- Molecule
- Transmembrane protein 94
- UniProt
- Q12767
- Pockets
- 16 · best druggability 0.83
Structure
1 distinct chain · 44% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transmembrane protein 94 | protein | 1356 | 44% helix, 11% strand | Q12767 |
Pockets
16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1053 | 0.83 | 0.84 | 117 | empty |
| 2 | 1190 | 0.83 | 0.83 | 84 | empty |
| 3 | 916 | 0.77 | 0.80 | 92 | empty |
| 4 | 79 | 0.74 | 0.98 | 24 | empty |
| 5 | 345 | 0.72 | 0.84 | 54 | empty |
Modifications
Observed in the structure: 2 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 Q12767
- Elsewhere: UniProt Q12767 · AlphaFold DB Q12767
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