› 2vct

X-ray diffraction
2.1Å resolution

Glutathione transferase A2-2 in complex with delta-4-andostrene-3-17- dione

Released:
DOI: 10.2210/pdb2vct/pdb
PDB entry 2vct coloured by chain, front view.
PDB entry 2vct coloured by chain, side view.
PDB entry 2vct coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases.
Tars K, Olin B, Mannervik B
J Mol Biol 397 332-40 (2010)
PMID: 20083122

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A2 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 222 amino acids
Theoretical weight: 25.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09210 (Residues: 1-222; Coverage: 100%)
Gene names: GST2, GSTA2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ASD 4 x ASD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 105.546Å b: 97.343Å c: 110.302Å
α: 90° β: 115° γ: 90°
R-values:
R R work R free
0.221 0.217 0.288
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
6 more

2 mentions without citation

DeepDrug3D: Classification of ligand-binding pockets in proteins with a convolutional neural network.
Pu et al. (2019)
1 more