› 2jl4

X-ray diffraction
2.3Å resolution

Holo structure of Maleyl Pyruvate Isomerase, a bacterial glutathione- s-transferase in Zeta class

Released:
DOI: 10.2210/pdb2jl4/pdb
PDB 2jl4 coloured by chain and viewed from the front.
PDB 2jl4 coloured by chain and viewed from the side.
PDB 2jl4 coloured by chain and viewed from the top.
Source organism: Ralstonia sp. U2
Primary publication:
Structure of bacterial glutathione-S-transferase maleyl pyruvate isomerase and implications for mechanism of isomerisation.
Marsh M, Shoemark DK, Jacob A, Robinson C, Cahill B, Zhou NY, Williams PA, Hadfield AT
J. Mol. Biol. 384 165-77 (2008)
PMID: 18824004

Function and Biology Details

Reaction catalysed: 
3-maleylpyruvate = 3-fumarylpyruvate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Maleylpyruvate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 213 amino acids
Theoretical weight: 23.66 KDa
Source organism: Ralstonia sp. U2
Expression system: Escherichia coli
UniProt:
  • Canonical: O86043 (Residues: 1-212; Coverage: 100%)
Gene name: nagL
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P212121
Unit cell:
a: 60.332Å b: 81.733Å c: 88.187Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.211 0.267
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases.
Sylvestre-Gonon et al. (2019)
4 more