1ufy

X-ray diffraction
0.96Å resolution

Crystal analysis of chorismate mutase from thermus thermophilus

Released:
Source organism: Thermus thermophilus HB8
Entry authors: Inagaki E, 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

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chorismate mutase AroH Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 13.67 KDa
Source organism: Thermus thermophilus HB8
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

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: R32
Unit cell:
a: 71.252Å b: 71.252Å c: 152.36Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.11 0.11 0.127
Expression system: Escherichia coli BL21(DE3)