Research workbench
AlphaFold monomer V2.0 prediction for nicotinate phosphoribosyltransferase (Q5F836)
Analyse AlphaFold monomer V2.0 prediction for nicotinate phosphoribosyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5F836
- Type
- protein
- Length
- 402 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Nicotinate phosphoribosyltransferase
- UniProt
- Q5F836
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nicotinate phosphoribosyltransferase | protein | 402 | 49% helix, 15% strand | Q5F836 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 367 | 0.76 | 0.87 | 40 | empty |
| 2 | 178 | 0.56 | 0.80 | 30 | empty |
| 3 | 61 | 0.35 | 0.78 | 16 | empty |
| 4 | 58 | 0.29 | 0.75 | 18 | 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 Q5F836
- Elsewhere: UniProt Q5F836 · AlphaFold DB Q5F836
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