Research workbench
AlphaFold monomer V2.0 prediction for N-carbamoyl-L-amino-acid hydrolase (Q9F464)
Analyse AlphaFold monomer V2.0 prediction for N-carbamoyl-L-amino-acid hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9F464
- Type
- protein
- Length
- 412 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x27e67Efe562B17F05415cb640674a08713e14067
- Molecule
- N-carbamoyl-L-amino-acid hydrolase
- UniProt
- Q9F464
- Pockets
- 2 · best druggability 0.46
Structure
1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-carbamoyl-L-amino-acid hydrolase | protein | 412 | 37% helix, 24% strand | Q9F464 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.46 | 0.78 | 16 | empty |
| 2 | 167 | 0.44 | 0.75 | 35 | 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 Q9F464
- Elsewhere: UniProt Q9F464 · AlphaFold DB Q9F464
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