Research workbench
AlphaFold monomer V2.0 prediction for phosphoglucomutase (Q4L9R5)
Analyse AlphaFold monomer V2.0 prediction for phosphoglucomutase (Q4L9R5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4L9R5
- Type
- protein
- Length
- 548 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xadb39D07D2A55093085fD524c504c34Fc55E839E
- Molecule
- Phosphoglucomutase
- UniProt
- Q4L9R5
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucomutase | protein | 548 | 40% helix, 22% strand | Q4L9R5 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 962 | 0.74 | 0.77 | 86 | empty |
| 2 | 100 | 0.43 | 0.78 | 25 | empty |
| 3 | 86 | 0.35 | 0.75 | 20 | empty |
| 4 | 67 | 0.31 | 0.74 | 14 | 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 Q4L9R5
- Elsewhere: UniProt Q4L9R5 · AlphaFold DB Q4L9R5
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