Research workbench
FERREDOXIN:NADP+ oxidoreductase (ferredoxin reductase) mutant E312Q
Analyse FERREDOXIN:NADP+ oxidoreductase (ferredoxin reductase) mutant E312Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BX1
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (FERREDOXIN:NADP+ oxidoreductase)
- EC
- 1.18.1.2
- UniProt
- P00455
- Ligands
- FAD, PO4, SO4
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (FERREDOXIN:NADP+ oxidoreductase) (EC 1.18.1.2) | protein | 296 | 26% helix, 30% strand | P00455 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 287 | 0.56 | 0.76 | 42 | FAD |
Compared structures
- 1BX1 · FERREDOXIN:NADP+ oxidoreductase (ferredoxin reductase) mutant E312Q · the same entry in another collection · chain A against A, TM-score 1.00
- P00455 · AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase, chloroplastic (P00455) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P00455
- Elsewhere: RCSB PDB 1BX1 · PDBe 1BX1 · UniProt P00455
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