› 2ht9

X-ray diffraction
1.9Å resolution

The structure of dimeric human glutaredoxin 2

Released:
DOI: 10.2210/pdb2ht9/pdb
PDB entry 2ht9 coloured by chain, front view.
PDB entry 2ht9 coloured by chain, side view.
PDB entry 2ht9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria.
Johansson C, Kavanagh KL, Gileadi O, Oppermann U
J Biol Chem 282 3077-82 (2007)
PMID: 17121859

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162733 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutaredoxin-2, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 146 amino acids
Theoretical weight: 16.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NS18 (Residues: 41-164; Coverage: 76%)
Gene names: CGI-133, GLRX2, GRX2
Sequence domains: Glutaredoxin
Structure domains: Glutaredoxin
12-mer peptide Chain: X
Molecule details ›
Chain: X
Length: 12 amino acids
Theoretical weight: 1.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

2 bound ligands:
Ligand GSH 2 x GSH
Ligand FES 1 x FES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P63
Unit cell:
a: 111.754Å b: 111.754Å c: 51.647Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.149 0.178
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

22 review citations

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

13 mentions without citation

Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling.
Hanschmann et al. (2013)
12 more