› 1fnk

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE ANALYSIS OF CHORISMATE MUTASE MUTANT C88K/R90S

Released:
DOI: 10.2210/pdb1fnk/pdb
PDB entry 1fnk coloured by chain, front view.
PDB entry 1fnk coloured by chain, side view.
PDB entry 1fnk coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase.
Kast P, Grisostomi C, Chen IA, Li S, Krengel U, Xue Y, Hilvert D
J Biol Chem 275 36832-8 (2000)
PMID: 10960481

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148491 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chorismate mutase AroH Chain: A
Molecule details ›
Chain: A
Length: 127 amino acids
Theoretical weight: 14.5 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: RutC-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R3
Unit cell:
a: 82.5Å b: 82.5Å c: 42.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 0.251
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Aminobenzoates as building blocks for natural product assembly lines.
Walsh et al. (2012)
5 more

2 mentions without citation

Recognition of functional sites in protein structures.
Shulman-Peleg et al. (2004)
1 more