Research workbench
AlphaFold monomer V2.0 prediction for N-acetyl-gamma-glutamyl- phosphate reductase (A0KFV0)
Analyse AlphaFold monomer V2.0 prediction for N-acetyl-gamma-glutamyl- phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0KFV0
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ac19BF43ac46e707bF48e314206299eb9b460D6
- Molecule
- N-acetyl-gamma-glutamyl-phosphate reductase
- UniProt
- A0KFV0
- Pockets
- 2 · best druggability 0.69
Structure
1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyl-gamma-glutamyl-phosphate reductase | protein | 335 | 38% helix, 23% strand | A0KFV0 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 462 | 0.69 | 0.80 | 57 | empty |
| 2 | 50 | 0.26 | 0.73 | 15 | 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 A0KFV0
- Elsewhere: UniProt A0KFV0 · AlphaFold DB A0KFV0
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