› 1rql

X-ray diffraction
2.4Å resolution

Crystal Structure of Phosponoacetaldehyde Hydrolase Complexed with Magnesium and the Inhibitor Vinyl Sulfonate

Released:
DOI: 10.2210/pdb1rql/pdb
PDB entry 1rql coloured by chain, front view.
PDB entry 1rql coloured by chain, side view.
PDB entry 1rql coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis.
Morais MC, Zhang G, Zhang W, Olsen DB, Dunaway-Mariano D, Allen KN
J Biol Chem 279 9353-61 (2004)
PMID: 14670958

Function and Biology Details

Reaction catalysed: 
Phosphonoacetaldehyde + H(2)O = acetaldehyde + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128269 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphonoacetaldehyde hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 267 amino acids
Theoretical weight: 30.51 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: O31156 (Residues: 1-264; Coverage: 100%)
Gene name: phnX
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand VSO 1 x VSO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: C2
Unit cell:
a: 209.97Å b: 45.27Å c: 64.63Å
α: 90° β: 104.92° γ: 90°
R-values:
R R work R free
0.227 0.227 0.282
Expression system: Escherichia coli

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Citations

3 review citations

New ways to break an old bond: the bacterial carbon-phosphorus hydrolases and their role in biogeochemical phosphorus cycling.
Quinn et al. (2007)
2 more

1 mention without citation

Protein subunit interfaces: heterodimers versus homodimers.
Zhanhua et al. (2005)