MolNFT v1 · #257351 · protein
AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (A3D5M3)
A3D5M3: “AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (A3D5M3)”. 3 pockets (best druggability 0.81). MolNFT v1 #257351 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A3D5M3
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x281a6B0837cBc4ed623904D317162712731B3e50
- Molecule
- NH(3)-dependent NAD(+) synthetase
- UniProt
- A3D5M3
- Pockets
- 3 · best druggability 0.81
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 | A3D5M3 |
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 | 397 | 0.81 | 0.90 | 53 | empty |
| 2 | 55 | 0.35 | 0.78 | 14 | empty |
| 3 | 89 | 0.35 | 0.74 | 20 | 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 A3D5M3
- Elsewhere: UniProt A3D5M3 · AlphaFold DB A3D5M3
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