› 2aaq

X-ray diffraction
2.6Å resolution

Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI

Released:
DOI: 10.2210/pdb2aaq/pdb
PDB entry 2aaq coloured by chain, front view.
PDB entry 2aaq coloured by chain, side view.
PDB entry 2aaq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Undressing of phosphine gold(I) complexes as irreversible inhibitors of human disulfide reductases.
Urig S, Fritz-Wolf K, Réau R, Herold-Mende C, Tóth K, Davioud-Charvet E, Becker K
Angew Chem Int Ed Engl 45 1881-6 (2006)
PMID: 16493712

Function and Biology Details

Reaction catalysed: 
2 glutathione + NADP(+) = glutathione disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence 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: 479 amino acids
Theoretical weight: 51.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00390 (Residues: 44-522; Coverage: 92%)
Gene names: GLUR, GRD1, GSR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
6 bound ligands:
Ligand PO4 4 x PO4
Ligand CL 1 x CL
Ligand K 1 x K
Ligand AUP 1 x AUP
Ligand AU 2 x AU
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2
Unit cell:
a: 120.31Å b: 62.72Å c: 83.99Å
α: 90° β: 122.47° γ: 90°
R-values:
R R work R free
0.201 0.201 0.259
Expression system: Escherichia coli

Quick links

Citations

13 review citations

On the potential of thioredoxin reductase inhibitors for cancer therapy.
Urig et al. (2006)
12 more

4 mentions without citation

New trends for metal complexes with anticancer activity.
Bruijnincx et al. (2008)
3 more