› 3ct2

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
(+)-muconolactone = cis,cis-muconate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-175608 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mandelate racemase/muconate lactonizing enzyme C-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 382 amino acids
Theoretical weight: 41.05 KDa
Source organism: Pseudomonas protegens Pf-5
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4K9X1 (Residues: 2-372; Coverage: 97%)
Gene names: PFL_3862, catB
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P4212
Unit cell:
a: 135.928Å b: 135.928Å c: 82.968Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.222
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Directed evolution drives the next generation of biocatalysts.
Turner NJ. (2009)
6 more

1 mention without citation

Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes.
Sakai et al. (2009)