› 2v5k

X-ray diffraction
2.2Å resolution

Class II aldolase HpcH - magnesium - oxamate complex

Released:
DOI: 10.2210/pdb2v5k/pdb
PDB entry 2v5k coloured by chain, front view.
PDB entry 2v5k coloured by chain, side view.
PDB entry 2v5k coloured by chain, top view.
Source organism: Escherichia coli C
Primary publication:
Structure and mechanism of HpcH: a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli.
Rea D, Fülöp V, Bugg TD, Roper DI
J Mol Biol 373 866-76 (2007)
PMID: 17881002

Function and Biology Details

Reaction catalysed: 
4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175214 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-2-oxo-heptane-1,7-dioate aldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 287 amino acids
Theoretical weight: 31.14 KDa
Source organism: Escherichia coli C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47098 (Residues: 1-262; Coverage: 100%)
Gene names: hpaI, hpcH
Sequence domains: HpcH/HpaI aldolase/citrate lyase family
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand OXM 2 x OXM
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P213
Unit cell:
a: 152.2Å b: 152.2Å c: 152.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 0.192
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase.
Rakus et al. (2008)
8 more

2 mentions without citation

Structural and kinetic characterization of 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase, a protocatechuate degradation enzyme evolutionarily convergent with the HpaI and DmpG pyruvate aldolases.
Wang et al. (2010)
1 more