› 1md4

X-ray diffraction
2.1Å resolution

A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to valine

Released:
DOI: 10.2210/pdb1md4/pdb
PDB entry 1md4 coloured by chain, front view.
PDB entry 1md4 coloured by chain, side view.
PDB entry 1md4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Contribution of glycine 146 to a conserved folding module affecting stability and refolding of human glutathione transferase p1-1.
Kong GK, Polekhina G, McKinstry WJ, Parker MW, Dragani B, Aceto A, Paludi D, Principe DR, Mannervik B, Stenberg G
J Biol Chem 278 1291-302 (2003)
PMID: 12414796

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-140593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase P Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 23.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 2-210; Coverage: 100%)
Gene names: FAEES3, GST3, GSTP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
1 bound ligand:
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 77.27Å b: 89.44Å c: 68.92Å
α: 90° β: 98.07° γ: 90°
R-values:
R R work R free
0.207 0.207 0.235
Expression system: Escherichia coli

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Citations

3 review citations

Insect glutathione transferases.
Ketterman et al. (2011)
2 more