3iac

X-ray diffraction
2.22Å resolution

2.2 Angstrom Crystal Structure of Glucuronate Isomerase from Salmonella typhimurium.

Released:
Entry authors: Minasov G, Wawrzak Z, Skarina T, Onopriyenko O, Peterson SN, Savchenko A, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

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-187270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uronate isomerase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 473 amino acids
Theoretical weight: 54.69 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ZM23 (Residues: 1-470; Coverage: 100%)
Gene names: STM3137, uxaC
Sequence domains: Glucuronate isomerase
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P42212
Unit cell:
a: 225.535Å b: 225.535Å c: 82.745Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.146 0.144 0.181
Expression system: Escherichia coli