Research workbench
AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (Q5NNT4)
Analyse AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (Q5NNT4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5NNT4
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
- Molecule
- Phosphoglucosamine mutase
- UniProt
- Q5NNT4
- Pockets
- 4 · best druggability 0.45
Structure
1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucosamine mutase | protein | 445 | 39% helix, 22% strand | Q5NNT4 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.45 | 0.83 | 18 | empty |
| 2 | 175 | 0.44 | 0.75 | 31 | empty |
| 3 | 60 | 0.31 | 0.75 | 13 | empty |
| 4 | 53 | 0.24 | 0.72 | 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 Q5NNT4
- Elsewhere: UniProt Q5NNT4 · AlphaFold DB Q5NNT4
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