Research workbench
AlphaFold monomer V2.0 prediction for mannose-P-dolichol utilization defect 1 protein (Q9R0Q9)
Analyse AlphaFold monomer V2.0 prediction for mannose-P-dolichol utilization defect 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9R0Q9
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf498a07CB267aF7A6C8376eAc13c07Cb31bc9C20
- Molecule
- Mannose-P-dolichol utilization defect 1 protein
- UniProt
- Q9R0Q9
- Pockets
- 2 · best druggability 0.66
Structure
1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mannose-P-dolichol utilization defect 1 protein | protein | 247 | 77% helix, 0% strand | Q9R0Q9 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 466 | 0.66 | 0.78 | 32 | empty |
| 2 | 54 | 0.30 | 0.75 | 12 | 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 Q9R0Q9
- Elsewhere: UniProt Q9R0Q9 · AlphaFold DB Q9R0Q9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.