Research workbench
AlphaFold monomer V2.0 prediction for nitrate reductase molybdenum cofactor assembly chaperone narj (P0AF27)
Analyse AlphaFold monomer V2.0 prediction for nitrate reductase molybdenum cofactor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0AF27
- Type
- protein
- Length
- 236 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- Nitrate reductase molybdenum cofactor assembly chaperone narj
- UniProt
- P0AF27
- Pockets
- 3 · best druggability 0.37
Structure
1 distinct chain · 61% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrate reductase molybdenum cofactor assembly chaperone narj | protein | 236 | 61% helix, 1% strand | P0AF27 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.37 | 0.76 | 22 | empty |
| 2 | 85 | 0.36 | 0.75 | 16 | empty |
| 3 | 57 | 0.34 | 0.78 | 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 P0AF27
- Elsewhere: UniProt P0AF27 · AlphaFold DB P0AF27
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