Research workbench
AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (Q7VZ59)
Analyse AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (Q7VZ59) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7VZ59
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8B076cFcCce75c7d28db718CD81F3160E1E1Ee20
- Molecule
- Phosphoglucosamine mutase
- UniProt
- Q7VZ59
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucosamine mutase | protein | 452 | 38% helix, 21% strand | Q7VZ59 |
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 | 51 | 0.65 | 0.95 | 24 | empty |
| 2 | 147 | 0.42 | 0.74 | 24 | empty |
| 3 | 101 | 0.37 | 0.75 | 21 | empty |
| 4 | 74 | 0.34 | 0.76 | 13 | 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 Q7VZ59
- Elsewhere: UniProt Q7VZ59 · AlphaFold DB Q7VZ59
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