5ti1

X-ray diffraction
2Å resolution

Crystal Structure of Fumarylacetoacetate hydrolase from Burkholderia xenovorans LB400

Released:
Entry authors: Seattle Structural Genomics Center for Infectious Disease, SSGCID, Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
4-fumarylacetoacetate + H(2)O = acetoacetate + fumarate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-556450 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
fumarylacetoacetase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 444 amino acids
Theoretical weight: 48.52 KDa
Source organism: Paraburkholderia xenovorans LB400
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q144Z1 (Residues: 1-436; Coverage: 100%)
Gene name: Bxe_A3899
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P1
Unit cell:
a: 65.9Å b: 83.1Å c: 186.29Å
α: 101.63° β: 91.17° γ: 113.81°
R-values:
R R work R free
0.155 0.154 0.199
Expression system: Escherichia coli BL21(DE3)