Research workbench
AlphaFold monomer V2.0 prediction for udp-3-O-acyl-N- acetylglucosamine deacetylase (Q7NQ05)
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
- Q7NQ05
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Udp-3-O-acyl-N-acetylglucosamine deacetylase
- UniProt
- Q7NQ05
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 25% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-3-O-acyl-N-acetylglucosamine deacetylase | protein | 304 | 25% helix, 32% strand | Q7NQ05 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.75 | 0.93 | 24 | empty |
| 2 | 317 | 0.65 | 0.80 | 42 | empty |
| 3 | 101 | 0.44 | 0.79 | 15 | empty |
| 4 | 79 | 0.42 | 0.80 | 22 | 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 Q7NQ05
- Elsewhere: UniProt Q7NQ05 · AlphaFold DB Q7NQ05
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