› 3gtu

X-ray diffraction
2.8Å resolution

LIGAND-FREE HETERODIMERIC HUMAN GLUTATHIONE S-TRANSFERASE M2-3 (EC 2.5.1.18), MONOCLINIC CRYSTAL FORM

Released:
DOI: 10.2210/pdb3gtu/pdb
PDB entry 3gtu coloured by chain, front view.
PDB entry 3gtu coloured by chain, side view.
PDB entry 3gtu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases.
Patskovsky YV, Patskovska LN, Listowsky I
Biochemistry 38 16187-94 (1999)
PMID: 10587441

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

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-149195 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione S-transferase Mu 2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 217 amino acids
Theoretical weight: 25.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28161 (Residues: 2-218; Coverage: 100%)
Gene names: GST4, GSTM2
Sequence domains:
Structure domains:
Glutathione S-transferase Mu 3 Chains: B, D
Molecule details ›
Chains: B, D
Length: 224 amino acids
Theoretical weight: 26.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21266 (Residues: 2-225; Coverage: 100%)
Gene names: GST5, GSTM3
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: P21
Unit cell:
a: 51.97Å b: 102.747Å c: 103.977Å
α: 90° β: 95.8° γ: 90°
R-values:
R R work R free
0.225 0.225 0.27
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Glutathione transferases.
Hayes et al. (2005)
1 more

3 mentions without citation

Structural similarity enhances interaction propensity of proteins.
Lukatsky et al. (2007)
2 more