MolNFT v1 · #257377 · protein
AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (Q5HEK9)
Q5HEK9: “AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (Q5HEK9)”. 3 pockets (best druggability 0.79). MolNFT v1 #257377 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q5HEK9
- Type
- protein
- Length
- 273 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- NH(3)-dependent NAD(+) synthetase
- UniProt
- Q5HEK9
- Pockets
- 3 · best druggability 0.79
Structure
1 distinct chain · 52% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NH(3)-dependent NAD(+) synthetase | protein | 273 | 52% helix, 8% strand | Q5HEK9 |
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 | 445 | 0.79 | 0.88 | 60 | empty |
| 2 | 52 | 0.34 | 0.78 | 14 | empty |
| 3 | 92 | 0.33 | 0.73 | 19 | empty |
Compared structures
- 6KV3 · Crystal structure of NAD+ synthetase from staphylococcus aureus · an experimental structure of the same protein · chain A against B, TM-score 0.91
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 Q5HEK9
- Elsewhere: UniProt Q5HEK9 · AlphaFold DB Q5HEK9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.