› 1grg

X-ray diffraction
2Å resolution

SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1grg/pdb
PDB entry 1grg coloured by chain, front view.
PDB entry 1grg coloured by chain, side view.
PDB entry 1grg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution.
Karplus PA, Schulz GE
J Mol Biol 210 163-80 (1989)
PMID: 2585516

Function and Biology Details

Reaction catalysed: 
2 glutathione + NADP(+) = glutathione disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132462 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione reductase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 478 amino acids
Theoretical weight: 51.74 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00390 (Residues: 45-522; Coverage: 92%)
Gene names: GLUR, GRD1, GSR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand PO4 1 x PO4
1 modified residue:
Ligand 0A8 1 x 0A8

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 119.8Å b: 84.5Å c: 63.2Å
α: 90° β: 90° γ: 58.7°
R-values:
R R work R free
0.168 not available not available
Expression system: Not provided

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Citations

18 review citations

Protein sulfenic acids in redox signaling.
Poole et al. (2004)
17 more

2 mentions without citation

Thioredoxin reductase and its inhibitors.
Saccoccia et al. (2014)
1 more