› 1hna

X-ray diffraction
1.85Å resolution

CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY

Released:
DOI: 10.2210/pdb1hna/pdb
PDB entry 1hna coloured by chain, front view.
PDB entry 1hna coloured by chain, side view.
PDB entry 1hna coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity.
Raghunathan S, Chandross RJ, Kretsinger RH, Allison TJ, Penington CJ, Rule GS
J Mol Biol 238 815-32 (1994)
PMID: 8182750

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-151172 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Mu 2 Chain: A
Molecule details ›
Chain: A
Length: 217 amino acids
Theoretical weight: 25.61 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P28161 (Residues: 2-218; Coverage: 100%)
Gene names: GST4, GSTM2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GDN 1 x GDN
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 81.19Å b: 83.52Å c: 70.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.226 not available
Expression system: Not provided

Quick links

Citations

7 review citations

Glutathione transferases, regulators of cellular metabolism and physiology.
Board et al. (2013)
6 more

5 mentions without citation

Sequence variations within protein families are linearly related to structural variations.
Koehl et al. (2002)
4 more