1ode

X-ray diffraction
1.65Å resolution

Crystal Analysis Of Chorismate Mutase From Thermus Thermophilus.

Released:
Source organism: Thermus thermophilus HB8
Entry authors: Inagaki E, Miyano M, Tahirov TH

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: 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

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P212121
Unit cell:
a: 47.319Å b: 78.54Å c: 86.035Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.239
Expression system: Escherichia coli BL21(DE3)