Research workbench
AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (A2RXU4)
Analyse AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (A2RXU4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2RXU4
- Type
- protein
- Length
- 284 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x17E9d21fd624B72bb4C36cf08735A72f9f3D109A
- Molecule
- NH(3)-dependent NAD(+) synthetase
- UniProt
- A2RXU4
- Pockets
- 2 · best druggability 0.82
Structure
1 distinct chain · 53% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NH(3)-dependent NAD(+) synthetase | protein | 284 | 53% helix, 8% strand | A2RXU4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 506 | 0.82 | 0.89 | 58 | empty |
| 2 | 136 | 0.42 | 0.75 | 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 A2RXU4
- Elsewhere: UniProt A2RXU4 · AlphaFold DB A2RXU4
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