Research workbench
AlphaFold monomer V2.0 prediction for quinolinate synthase a (A5F769)
Analyse AlphaFold monomer V2.0 prediction for quinolinate synthase a (A5F769) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5F769
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe76b3F28d48eB037bFBabB880119B8b2f3E26Fb5
- Molecule
- Quinolinate synthase a
- UniProt
- A5F769
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Quinolinate synthase a | protein | 353 | 47% helix, 15% strand | A5F769 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.77 | 0.98 | 28 | empty |
| 2 | 195 | 0.46 | 0.75 | 28 | empty |
| 3 | 78 | 0.32 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 A5F769
- Elsewhere: UniProt A5F769 · AlphaFold DB A5F769
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