Research workbench
AlphaFold monomer V2.0 prediction for nitrate reductase [NADH] 2 (P11035)
Analyse AlphaFold monomer V2.0 prediction for nitrate reductase [NADH] 2 (P11035) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P11035
- Type
- protein
- Length
- 917 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdED03e95F08d927Dab208C6936D4158E4a542f89
- Molecule
- Nitrate reductase [NADH] 2
- UniProt
- P11035
- Pockets
- 12 · best druggability 0.75
Structure
1 distinct chain · 22% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrate reductase [NADH] 2 | protein | 917 | 22% helix, 28% strand | P11035 |
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 859 | 0.75 | 0.78 | 80 | empty |
| 2 | 226 | 0.73 | 0.88 | 43 | empty |
| 3 | 372 | 0.66 | 0.80 | 36 | empty |
| 4 | 242 | 0.61 | 0.81 | 26 | empty |
| 5 | 195 | 0.55 | 0.79 | 31 | 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 P11035
- Elsewhere: UniProt P11035 · AlphaFold DB P11035
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