› 2v5j

X-ray diffraction
1.6Å resolution

Apo Class II aldolase HpcH

Released:
DOI: 10.2210/pdb2v5j/pdb
PDB entry 2v5j coloured by chain, front view.
PDB entry 2v5j coloured by chain, side view.
PDB entry 2v5j 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-559528 (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

2 bound ligands:
Ligand PO4 2 x PO4
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: R32
Unit cell:
a: 128.92Å b: 128.92Å c: 175.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.173 0.207
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

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

4 mentions without citation

The coxsackievirus-adenovirus receptor reveals complex homophilic and heterophilic interactions on neural cells.
Patzke et al. (2010)
3 more