2q01

X-ray diffraction
2.34Å resolution

Crystal structure of glucuronate isomerase from Caulobacter crescentus

Released:
Source organism: Caulobacter vibrioides CB15
Entry authors: Patskovsky Y, Bonanno J, Sridhar V, Sauder JM, Freeman J, Powell A, Koss J, Groshong C, Gheyi T, Wasserman SR, Raushel F, Burley SK, Almo SC, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed:
D-glucuronate = D-fructuronate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189499 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uronate isomerase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 497 amino acids
Theoretical weight: 56.34 KDa
Source organism: Caulobacter vibrioides CB15
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9A874 (Residues: 2-487; Coverage: 100%)
Gene names: CC_1490, uxaC
Sequence domains: Glucuronate isomerase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: F222
Unit cell:
a: 177.332Å b: 190.176Å c: 319.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.251
Expression system: Escherichia coli BL21(DE3)