› 2gbb

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
Chorismate = prephenate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Secreted chorismate mutase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 156 amino acids
Theoretical weight: 17.71 KDa
Source organism: Yersinia pestis biovar Microtus str. 91001
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7CHH5 (Residues: 31-186; Coverage: 100%)
Gene names: YPO1353, YP_1243, pheA2, y2828
Sequence domains: Chorismate mutase type II
Structure domains: Chorismate mutase

Ligands and Environments

2 bound ligands:
Ligand SO4 13 x SO4
Ligand CIT 4 x CIT
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2221
Unit cell:
a: 89.01Å b: 144.09Å c: 116.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.258
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Mycobacterium tuberculosis chorismate mutase: A potential target for TB.
Khanapur et al. (2017)
9 other articles

7 mentions without citation

A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis.
Kim et al. (2008)
6 more