Research workbench
AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (Q98PU6)
Analyse AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (Q98PU6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q98PU6
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA3982b0D16daaC5E84d2174159ed91c4Ce1827a7
- Molecule
- NH(3)-dependent NAD(+) synthetase
- UniProt
- Q98PU6
- Pockets
- 1 · best druggability 0.78
Structure
1 distinct chain · 54% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NH(3)-dependent NAD(+) synthetase | protein | 257 | 54% helix, 8% strand | Q98PU6 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 652 | 0.78 | 0.83 | 74 | 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 Q98PU6
- Elsewhere: UniProt Q98PU6 · AlphaFold DB Q98PU6
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