Research workbench
AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (C1L207)
Analyse AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (C1L207) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C1L207
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- NH(3)-dependent NAD(+) synthetase
- UniProt
- C1L207
- Pockets
- 3 · best druggability 0.81
Structure
1 distinct chain · 53% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NH(3)-dependent NAD(+) synthetase | protein | 274 | 53% helix, 8% strand | C1L207 |
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 | 554 | 0.81 | 0.87 | 66 | empty |
| 2 | 79 | 0.34 | 0.75 | 18 | empty |
| 3 | 52 | 0.30 | 0.76 | 15 | 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 C1L207
- Elsewhere: UniProt C1L207 · AlphaFold DB C1L207
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