1i7o

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF HPCE

Released:
Source organism: Escherichia coli
Entry authors: Tame JRH, Namba K, Dodson EJ, Roper DI

Function and Biology Details

Reactions catalysed:
(1a) (3E,5R)-5-carboxy-2-oxohept-3-enedioate = (4Z)-2-hydroxyhepta-2,4-dienedioate + CO(2)
5-carboxymethyl-2-hydroxymuconate = (3E,5R)-5-carboxy-2-oxohept-3-enedioate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-153400 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 429 amino acids
Theoretical weight: 47.15 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P37352 (Residues: 1-402, 403-427; Coverage: 100%)
Gene name: hpcE
Sequence domains: Fumarylacetoacetate (FAA) hydrolase family
Structure domains: Fumarylacetoacetase-like, C-terminal domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 126.084Å b: 138.201Å c: 103.973Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.251 0.278
Expression system: Escherichia coli