Research workbench
AlphaFold monomer V2.0 prediction for glutamine-dependent NAD(+) synthetase (Q9X0Y0)
Analyse AlphaFold monomer V2.0 prediction for glutamine-dependent NAD(+) synthetase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9X0Y0
- Type
- protein
- Length
- 576 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc7289c3ff1CD901cF20482f898aA0720155C409f
- Molecule
- Glutamine-dependent NAD(+) synthetase
- UniProt
- Q9X0Y0
- Pockets
- 8 · best druggability 0.82
Structure
1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine-dependent NAD(+) synthetase | protein | 576 | 40% helix, 19% strand | Q9X0Y0 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.82 | 0.90 | 59 | empty |
| 2 | 57 | 0.58 | 0.90 | 16 | empty |
| 3 | 73 | 0.47 | 0.83 | 17 | empty |
| 4 | 94 | 0.46 | 0.80 | 17 | empty |
| 5 | 132 | 0.43 | 0.76 | 18 | 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 Q9X0Y0
- Elsewhere: UniProt Q9X0Y0 · AlphaFold DB Q9X0Y0
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