› 4gr1

X-ray diffraction
2.4Å resolution

THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE

Released:
DOI: 10.2210/pdb4gr1/pdb
PDB entry 4gr1 coloured by chain, front view.
PDB entry 4gr1 coloured by chain, side view.
PDB entry 4gr1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The binding of the retro-analogue of glutathione disulfide to glutathione reductase.
Janes W, Schulz GE
J Biol Chem 265 10443-5 (1990)
PMID: 2355009

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 RGS 1 x RGS
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
0.151 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Prediction of binding constants of protein ligands: a fast method for the prioritization of hits obtained from de novo design or 3D database search programs.
Böhm HJ. (1998)
1 more

4 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
3 more