Research workbench
AlphaFold monomer V2.0 prediction for glutamine-dependent NAD(+) synthetase (P38795)
Analyse AlphaFold monomer V2.0 prediction for glutamine-dependent NAD(+) synthetase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P38795
- Type
- protein
- Length
- 714 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Glutamine-dependent NAD(+) synthetase
- UniProt
- P38795
- Pockets
- 7 · best druggability 0.82
Structure
1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine-dependent NAD(+) synthetase | protein | 714 | 45% helix, 18% strand | P38795 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 634 | 0.82 | 0.87 | 60 | empty |
| 2 | 69 | 0.55 | 0.88 | 18 | empty |
| 3 | 186 | 0.52 | 0.78 | 19 | empty |
| 4 | 72 | 0.39 | 0.78 | 19 | empty |
| 5 | 68 | 0.35 | 0.77 | 14 | 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 P38795
- Elsewhere: UniProt P38795 · AlphaFold DB P38795
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