› 1grf

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/pdb1grf/pdb
PDB entry 1grf coloured by chain, front view.
PDB entry 1grf coloured by chain, side view.
PDB entry 1grf 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: 51.64 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
2 bound ligands:
Ligand PO4 1 x PO4
Ligand ACM 1 x ACM
No modified residues

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
0.164 not available not available
Expression system: Not provided

Quick links

Citations

19 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
18 more

1 mention without citation

An Activity-Guided Map of Electrophile-Cysteine Interactions in Primary Human T Cells.
Vinogradova et al. (2020)