Research workbench
AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (C3LUM7)
Analyse AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (C3LUM7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3LUM7
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- NH(3)-dependent NAD(+) synthetase
- UniProt
- C3LUM7
- Pockets
- 4 · best druggability 0.82
Structure
1 distinct chain · 54% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NH(3)-dependent NAD(+) synthetase | protein | 276 | 54% helix, 8% strand | C3LUM7 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 509 | 0.82 | 0.88 | 65 | empty |
| 2 | 72 | 0.35 | 0.76 | 13 | empty |
| 3 | 53 | 0.34 | 0.78 | 13 | empty |
| 4 | 80 | 0.32 | 0.73 | 19 | 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 C3LUM7
- Elsewhere: UniProt C3LUM7 · AlphaFold DB C3LUM7
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