› 1gtu

X-ray diffraction
2.68Å resolution

LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M1A-1A

Released:
DOI: 10.2210/pdb1gtu/pdb
PDB entry 1gtu coloured by chain, front view.
PDB entry 1gtu coloured by chain, side view.
PDB entry 1gtu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a.
Patskovsky YV, Patskovska LN, Listowsky I
Biochemistry 38 1193-202 (1999)
PMID: 9930979

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
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-140674 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Mu 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 217 amino acids
Theoretical weight: 25.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09488 (Residues: 2-218; Coverage: 100%)
Gene names: GST1, GSTM1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 56.957Å b: 84.987Å c: 215.382Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.245
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Human cytosolic glutathione-S-transferases: quantitative analysis of expression, comparative analysis of structures and inhibition strategies of isozymes involved in drug resistance.
Mohana et al. (2017)
16 other articles

5 mentions without citation

X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum.
Fritz-Wolf et al. (2003)
4 more