Research workbench
AlphaFold monomer V2.0 prediction for assimilatory nitrate reductase catalytic subunit (P42434)
Analyse AlphaFold monomer V2.0 prediction for assimilatory nitrate reductase catalytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P42434
- Type
- protein
- Length
- 710 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Assimilatory nitrate reductase catalytic subunit
- UniProt
- P42434
- Pockets
- 6 · best druggability 0.88
Structure
1 distinct chain · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Assimilatory nitrate reductase catalytic subunit | protein | 710 | 37% helix, 20% strand | P42434 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 384 | 0.88 | 0.97 | 74 | empty |
| 2 | 67 | 0.46 | 0.83 | 18 | empty |
| 3 | 75 | 0.41 | 0.79 | 23 | empty |
| 4 | 138 | 0.40 | 0.74 | 24 | empty |
| 5 | 88 | 0.35 | 0.74 | 13 | 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 P42434
- Elsewhere: UniProt P42434 · AlphaFold DB P42434
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