Research workbench
AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (Q49YV6)
Analyse AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (Q49YV6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q49YV6
- Type
- protein
- Length
- 273 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC3139F25753039810c47bBeCF44703fF28C29Fd6
- Molecule
- NH(3)-dependent NAD(+) synthetase
- UniProt
- Q49YV6
- Pockets
- 3 · best druggability 0.80
Structure
1 distinct chain · 51% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NH(3)-dependent NAD(+) synthetase | protein | 273 | 51% helix, 8% strand | Q49YV6 |
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 | 500 | 0.80 | 0.87 | 64 | empty |
| 2 | 100 | 0.34 | 0.73 | 20 | empty |
| 3 | 59 | 0.34 | 0.77 | 12 | 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 Q49YV6
- Elsewhere: UniProt Q49YV6 · AlphaFold DB Q49YV6
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