Research workbench
AlphaFold monomer V2.0 prediction for acetylornithine deacetylase (Q57H96)
Analyse AlphaFold monomer V2.0 prediction for acetylornithine deacetylase (Q57H96) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q57H96
- Type
- protein
- Length
- 383 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Acetylornithine deacetylase
- UniProt
- Q57H96
- Pockets
- 1 · best druggability 0.44
Structure
1 distinct chain · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylornithine deacetylase | protein | 383 | 32% helix, 24% strand | Q57H96 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 164 | 0.44 | 0.75 | 23 | 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 Q57H96
- Elsewhere: UniProt Q57H96 · AlphaFold DB Q57H96
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