› 2vcv

X-ray diffraction
1.8Å resolution

Glutathione transferase A3-3 in complex with glutathione and delta-4- androstene-3-17-dione

Released:
DOI: 10.2210/pdb2vcv/pdb
PDB entry 2vcv coloured by chain, front view.
PDB entry 2vcv coloured by chain, side view.
PDB entry 2vcv 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-172573 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A3 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 222 amino acids
Theoretical weight: 25.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16772 (Residues: 1-222; Coverage: 100%)
Gene name: GSTA3
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 16 x GSH
1 bound ligand:
Ligand ASD 11 x ASD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P1
Unit cell:
a: 90.177Å b: 92.064Å c: 113.54Å
α: 89.76° β: 89.72° γ: 89.73°
R-values:
R R work R free
0.225 0.223 0.267
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

7 mentions without citation

Glutathione Transferases as Efficient Ketosteroid Isomerases.
Mannervik et al. (2021)
6 more