Research workbench
AlphaFold monomer V2.0 prediction for vacuolar membrane protein YPL162C (Q12042)
Analyse AlphaFold monomer V2.0 prediction for vacuolar membrane protein YPL162C (Q12042) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12042
- Type
- protein
- Length
- 273 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Vacuolar membrane protein YPL162C
- UniProt
- Q12042
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 68% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar membrane protein YPL162C | protein | 273 | 68% helix, 1% strand | Q12042 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 716 | 0.70 | 0.77 | 58 | empty |
| 2 | 120 | 0.52 | 0.81 | 22 | empty |
| 3 | 144 | 0.44 | 0.76 | 27 | 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 Q12042
- Elsewhere: UniProt Q12042 · AlphaFold DB Q12042
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