8ebc

X-ray diffraction
2.5Å resolution

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Listeria monocytogenes in the complex with IMP

Released:
Source organism: Listeria monocytogenes EGD-e
Entry authors: Kim Y, Maltseva N, Makowska-Grzyska M, Osipiuk J, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo hexamer
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CBS domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 395 amino acids
Theoretical weight: 43.08 KDa
Source organism: Listeria monocytogenes EGD-e
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8YAJ3 (Residues: 1-100, 212-502; Coverage: 78%)
Gene name: lmo0132
Sequence domains: IMP dehydrogenase / GMP reductase domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 78.977Å b: 95.699Å c: 97.604Å
α: 111.36° β: 105.17° γ: 107.61°
R-values:
R R work R free
0.196 0.194 0.239
Expression system: Escherichia coli BL21(DE3)