3kuu

X-ray diffraction
1.41Å resolution

Structure of the PurE Phosphoribosylaminoimidazole Carboxylase Catalytic Subunit from Yersinia pestis

Released:
Source organism: Yersinia pestis
Entry authors: Anderson SM, Wawrzak Z, Brunzelle JS, Onopriyenko O, Kwon K, Edwards A, Savchenko A, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo octamer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N5-carboxyaminoimidazole ribonucleotide mutase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 174 amino acids
Theoretical weight: 18.24 KDa
Source organism: Yersinia pestis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A384KAN6 (Residues: 1-174; Coverage: 100%)
Gene names: YPO3076, purE
Structure domains: PurE domain

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: I422
Unit cell:
a: 114.04Å b: 114.04Å c: 231.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.15 0.167
Expression system: Escherichia coli BL21(DE3)