6u7l

X-ray diffraction
2.75Å resolution

2.75 Angstrom Crystal Structure of Galactarate Dehydratase from Escherichia coli.

Released:
Source organism: Escherichia coli K-12
Entry authors: Minasov G, Shuvalova L, Wawrzak Z, Dubrovska I, Kiryukhina O, Endres M, Satchell KJF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
Galactarate = (2R,3S)-2,3-dihydroxy-5-oxohexanedioate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Galactarate dehydratase (L-threo-forming) Chains: A, B
Molecule details ›
Chains: A, B
Length: 526 amino acids
Theoretical weight: 57.33 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39829 (Residues: 1-523; Coverage: 100%)
Gene names: JW3097, b3128, garD, yhaG
Sequence domains:
Galactarate dehydratase (L-threo-forming) Chains: C, D
Molecule details ›
Chains: C, D
Length: 526 amino acids
Theoretical weight: 57.25 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39829 (Residues: 1-523; Coverage: 100%)
Gene names: JW3097, b3128, garD, yhaG
Sequence domains:

Ligands and Environments

2 bound ligands:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 58.462Å b: 167.574Å c: 117.065Å
α: 90° β: 103.97° γ: 90°
R-values:
R R work R free
0.208 0.206 0.241
Expression system: Escherichia coli BL21(DE3)