Research workbench
AlphaFold monomer V2.0 prediction for assimilatory ferredoxin- dependent nitrite reductase (I3R637)
Analyse AlphaFold monomer V2.0 prediction for assimilatory ferredoxin- dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- I3R637
- Type
- protein
- Length
- 586 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
- Molecule
- Assimilatory ferredoxin-dependent nitrite reductase
- UniProt
- I3R637
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Assimilatory ferredoxin-dependent nitrite reductase | protein | 586 | 36% helix, 22% strand | I3R637 |
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 | 609 | 0.80 | 0.85 | 62 | empty |
| 2 | 63 | 0.63 | 0.93 | 22 | empty |
| 3 | 111 | 0.44 | 0.78 | 18 | empty |
| 4 | 76 | 0.38 | 0.78 | 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 I3R637
- Elsewhere: UniProt I3R637 · AlphaFold DB I3R637
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