› 4maq

X-ray diffraction
1.4Å resolution

Crystal Structure of a putative fumarylpyruvate hydrolase from Burkholderia cenocepacia

Released:
DOI: 10.2210/pdb4maq/pdb
PDB entry 4maq coloured by chain, front view.
PDB entry 4maq coloured by chain, side view.
PDB entry 4maq coloured by chain, top view.
Source organism: Burkholderia cenocepacia J2315
Entry authors: Seattle Structural Genomics Center for Infectious Disease, Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110057 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fumarylacetoacetase-like C-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 240 amino acids
Theoretical weight: 25.78 KDa
Source organism: Burkholderia cenocepacia J2315
Expression system: Escherichia coli
UniProt:
  • Canonical: B4EKU2 (Residues: 1-232; Coverage: 100%)
Gene name: BCAM1692
Sequence domains: Fumarylacetoacetate (FAA) hydrolase family
Structure domains: Fumarylacetoacetase-like, C-terminal domain

Ligands and Environments

1 bound ligand:
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 51.17Å b: 51.63Å c: 186.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.134 0.132 0.168
Expression system: Escherichia coli

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