Research workbench
AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (A7X442)
Analyse AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (A7X442) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7X442
- Type
- protein
- Length
- 273 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- NH(3)-dependent NAD(+) synthetase
- UniProt
- A7X442
- Pockets
- 3 · best druggability 0.80
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 | A7X442 |
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 | 488 | 0.80 | 0.88 | 62 | empty |
| 2 | 97 | 0.36 | 0.74 | 21 | empty |
| 3 | 64 | 0.35 | 0.78 | 13 | 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 A7X442
- Elsewhere: UniProt A7X442 · AlphaFold DB A7X442
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