MolNFT v1 · #257425 · protein
AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (Q96YL5)
Q96YL5: “AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (Q96YL5)”. 2 pockets (best druggability 0.80). MolNFT v1 #257425 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q96YL5
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x045a1b77c52d845d6e7Ba6a444600C064C71354A
- Molecule
- NH(3)-dependent NAD(+) synthetase
- UniProt
- Q96YL5
- Pockets
- 2 · best druggability 0.80
Structure
1 distinct chain · 53% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NH(3)-dependent NAD(+) synthetase | protein | 279 | 53% helix, 7% strand | Q96YL5 |
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 | 505 | 0.80 | 0.86 | 72 | empty |
| 2 | 54 | 0.30 | 0.75 | 10 | 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 Q96YL5
- Elsewhere: UniProt Q96YL5 · AlphaFold DB Q96YL5
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