MolNFT v1 · #257144 · protein
AlphaFold monomer V2.0 prediction for glutamine-dependent NAD(+) synthetase (O67091)
O67091: “AlphaFold monomer V2.0 prediction for glutamine-dependent NAD(+) synthetase (O67091)”. 4 pockets (best druggability 0.79). MolNFT v1 #257144 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- O67091
- Type
- protein
- Length
- 567 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Glutamine-dependent NAD(+) synthetase
- UniProt
- O67091
- Pockets
- 4 · best druggability 0.79
Structure
1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine-dependent NAD(+) synthetase | protein | 567 | 41% helix, 19% strand | O67091 |
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 | 472 | 0.79 | 0.87 | 62 | empty |
| 2 | 74 | 0.40 | 0.78 | 18 | empty |
| 3 | 70 | 0.31 | 0.74 | 17 | empty |
| 4 | 54 | 0.29 | 0.75 | 16 | 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 O67091
- Elsewhere: UniProt O67091 · AlphaFold DB O67091
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