Research workbench
AlphaFold monomer V2.0 prediction for nitrate reductase [NADH] (P27967)
Analyse AlphaFold monomer V2.0 prediction for nitrate reductase [NADH] (P27967) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P27967
- Type
- protein
- Length
- 915 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe26BC75B33Cf508D508699DA6F01356e8b386510
- Molecule
- Nitrate reductase [NADH]
- UniProt
- P27967
- Pockets
- 12 · best druggability 0.74
Structure
1 distinct chain · 21% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrate reductase [NADH] | protein | 915 | 21% helix, 28% strand | P27967 |
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 | 832 | 0.74 | 0.78 | 92 | empty |
| 2 | 569 | 0.68 | 0.78 | 60 | empty |
| 3 | 378 | 0.65 | 0.80 | 35 | empty |
| 4 | 532 | 0.64 | 0.76 | 50 | empty |
| 5 | 129 | 0.56 | 0.83 | 23 | 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 P27967
- Elsewhere: UniProt P27967 · AlphaFold DB P27967
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