› 1tdi

X-ray diffraction
2.4Å resolution

Crystal Structure of hGSTA3-3 in Complex with Glutathione

Released:
DOI: 10.2210/pdb1tdi/pdb
PDB entry 1tdi coloured by chain, front view.
PDB entry 1tdi coloured by chain, side view.
PDB entry 1tdi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity.
Gu Y, Guo J, Pal A, Pan SS, Zimniak P, Singh SV, Ji X
Biochemistry 43 15673-9 (2004)
PMID: 15595823

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-172573 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 222 amino acids
Theoretical weight: 25.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q16772 (Residues: 1-222; Coverage: 100%)
Gene name: GSTA3
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 92.985Å b: 95.588Å c: 114.039Å
α: 90° β: 90.14° γ: 90°
R-values:
R R work R free
0.252 0.228 0.252
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

6 mentions without citation

Glutathione transferases are structural and functional outliers in the thioredoxin fold.
Atkinson et al. (2009)
5 more