Research workbench
AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (A4TRI7)
Analyse AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (A4TRI7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4TRI7
- Type
- protein
- Length
- 446 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7B18D86F87aA23e9a4c509ec729eD158010a5AD8
- Molecule
- Phosphoglucosamine mutase
- UniProt
- A4TRI7
- Pockets
- 2 · best druggability 0.56
Structure
1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucosamine mutase | protein | 446 | 39% helix, 22% strand | A4TRI7 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.56 | 0.85 | 19 | empty |
| 2 | 304 | 0.52 | 0.74 | 42 | 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 A4TRI7
- Elsewhere: UniProt A4TRI7 · AlphaFold DB A4TRI7
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