Research workbench
AlphaFold monomer V2.0 prediction for uncharacterized membrane protein YBR220C (P38318)
Analyse AlphaFold monomer V2.0 prediction for uncharacterized membrane protein YBR220C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P38318
- Type
- protein
- Length
- 560 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
- Molecule
- Uncharacterized membrane protein YBR220C
- UniProt
- P38318
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 69% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized membrane protein YBR220C | protein | 560 | 69% helix, 3% strand | P38318 |
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 | 1156 | 0.73 | 0.76 | 70 | empty |
| 2 | 295 | 0.63 | 0.80 | 41 | empty |
| 3 | 63 | 0.39 | 0.79 | 16 | empty |
| 4 | 51 | 0.25 | 0.72 | 13 | 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 P38318
- Elsewhere: UniProt P38318 · AlphaFold DB P38318
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