› 5zmu

X-ray diffraction
1.5Å resolution

Crystal structure of a cis-epoxysuccinate hydrolase producing D(-)-tartaric acids

Released:
DOI: 10.2210/pdb5zmu/pdb
PDB entry 5zmu coloured by chain, front view.
PDB entry 5zmu coloured by chain, side view.
PDB entry 5zmu coloured by chain, top view.
Source organism: Bordetella sp. BK-52
Primary publication:
Structural insight into the catalytic mechanism of a cis-epoxysuccinate hydrolase producing enantiomerically pure d(-)-tartaric acid.
Dong S, Liu X, Cui GZ, Cui Q, Wang X, Feng Y
Chem Commun (Camb) 54 8482-8485 (2018)
PMID: 30003205

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-514242 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cis-epoxysuccinate hydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 314 amino acids
Theoretical weight: 34.69 KDa
Source organism: Bordetella sp. BK-52
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: F1LJ99 (Residues: 1-294; Coverage: 100%)
Sequence domains: beta-keto acid cleavage enzyme

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P2
Unit cell:
a: 78.49Å b: 94.25Å c: 94.36Å
α: 90° β: 95.898° γ: 90°
R-values:
R R work R free
0.149 0.149 0.17
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Enantiomeric Tartaric Acid Production Using cis-Epoxysuccinate Hydrolase: History and Perspectives.
Xuan et al. (2019)
1 other article