PDBe 1dbf

X-ray diffraction
1.3Å resolution

CHORISMATE MUTASE FROM BACILLUS SUBTILIS AT 1.30 ANGSTROM

Released:
Source organism: Bacillus subtilis
Primary publication:
The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer.
Acta Crystallogr. D Biol. Crystallogr. 56 673-83 (2000)
PMID: 10818343

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chorismate mutase AroH Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 127 amino acids
Theoretical weight: 14.51 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P19080 (Residues: 1-127; Coverage: 100%)
Gene names: BSU22690, aroH
Sequence domains: Chorismate mutase type I
Structure domains: 60s Ribosomal Protein L30; Chain: A;

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 52.2Å b: 83.77Å c: 85.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 not available 0.235
Expression system: Escherichia coli