› 3rpp

X-ray diffraction
1.8Å resolution

Crystal structure of human kappa class glutathione transferase in apo form

Released:
DOI: 10.2210/pdb3rpp/pdb
PDB entry 3rpp coloured by chain, front view.
PDB entry 3rpp coloured by chain, side view.
PDB entry 3rpp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanism.
Wang B, Peng Y, Zhang T, Ding J
Biochem J 439 215-25 (2011)
PMID: 21728995

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195150 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase kappa 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 234 amino acids
Theoretical weight: 26.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y2Q3 (Residues: 1-226; Coverage: 100%)
Gene names: GSTK1, HDCMD47P
Sequence domains: DSBA-like thioredoxin domain
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2
Unit cell:
a: 146.113Å b: 84.29Å c: 87.316Å
α: 90° β: 122.12° γ: 90°
R-values:
R R work R free
0.154 0.152 0.195
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

3 mentions without citation

The Redox State Regulates the Conformation of Rv2466c to Activate the Antitubercular Prodrug TP053.
Albesa-Jové et al. (2015)
2 more