Research workbench
AlphaFold monomer V2.0 prediction for udp-3-O-acyl-N- acetylglucosamine deacetylase (Q9EV47)
Analyse AlphaFold monomer V2.0 prediction for udp-3-O-acyl-N- acetylglucosamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9EV47
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- Udp-3-O-acyl-N-acetylglucosamine deacetylase
- UniProt
- Q9EV47
- Pockets
- 3 · best druggability 0.66
Structure
1 distinct chain · 24% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-3-O-acyl-N-acetylglucosamine deacetylase | protein | 306 | 24% helix, 33% strand | Q9EV47 |
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 | 333 | 0.66 | 0.80 | 44 | empty |
| 2 | 181 | 0.62 | 0.83 | 36 | empty |
| 3 | 63 | 0.29 | 0.74 | 12 | 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 Q9EV47
- Elsewhere: UniProt Q9EV47 · AlphaFold DB Q9EV47
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