Research workbench
AlphaFold monomer V2.0 prediction for probable glucosamine 6-phosphate N-acetyltransferase (Q9VAI0)
Analyse AlphaFold monomer V2.0 prediction for probable glucosamine 6-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9VAI0
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x644EE9f2182e8e21d43CdeF48634b74F602D9E42
- Molecule
- Probable glucosamine 6-phosphate N-acetyltransferase
- UniProt
- Q9VAI0
- Pockets
- 3 · best druggability 0.52
Structure
1 distinct chain · 28% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable glucosamine 6-phosphate N-acetyltransferase | protein | 219 | 28% helix, 19% strand | Q9VAI0 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 232 | 0.52 | 0.76 | 32 | empty |
| 2 | 169 | 0.52 | 0.78 | 21 | empty |
| 3 | 193 | 0.48 | 0.75 | 25 | 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 Q9VAI0
- Elsewhere: UniProt Q9VAI0 · AlphaFold DB Q9VAI0
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