3nxl

X-ray diffraction
1.88Å resolution

Crystal structure of Glucarate dehydratase from Burkholderia cepacia complexed with magnesium

Released:
Source organism: Burkholderia lata
Entry authors: Fedorov AA, Fedorov EV, Gerlt JA, Burley SK, Almo SC, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed:
D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174468 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
glucarate dehydratase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 475 amino acids
Theoretical weight: 52.21 KDa
Source organism: Burkholderia lata
Expression system: Escherichia coli
UniProt:
  • Canonical: Q39KL8 (Residues: 2-465; Coverage: 100%)
Gene name: Bcep18194_A3396
Sequence domains: Enolase C-terminal domain-like
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 165.289Å b: 121.452Å c: 108.652Å
α: 90° β: 92.6° γ: 90°
R-values:
R R work R free
0.192 0.19 0.221
Expression system: Escherichia coli