1ui9

X-ray diffraction
1.65Å resolution

Crystal analysis of chorismate mutase from thermus thermophilus

Released:
Source organism: Thermus thermophilus
Entry authors: Inagaki E, Kuramitsu S, Yokoyama S, Miyano M, Tahirov TH, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo trimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183032 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chorismate mutase AroH Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 13.73 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q84FH6 (Residues: 1-122; Coverage: 100%)
Gene names: aroG, aroH
Sequence domains: Chorismate mutase type I
Structure domains: RutC-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P213
Unit cell:
a: 74.804Å b: 74.804Å c: 74.804Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.227
Expression system: Escherichia coli BL21(DE3)