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:

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
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)