› 1fez

X-ray diffraction
3Å resolution

THE CRYSTAL STRUCTURE OF BACILLUS CEREUS PHOSPHONOACETALDEHYDE HYDROLASE COMPLEXED WITH TUNGSTATE, A PRODUCT ANALOG

Released:
DOI: 10.2210/pdb1fez/pdb
PDB entry 1fez coloured by chain, front view.
PDB entry 1fez coloured by chain, side view.
PDB entry 1fez coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily.
Morais MC, Zhang W, Baker AS, Zhang G, Dunaway-Mariano D, Allen KN
Biochemistry 39 10385-96 (2000)
PMID: 10956028

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 256 amino acids
Theoretical weight: 29.16 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: O31156 (Residues: 2-257; Coverage: 97%)
Gene name: phnX
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand WO4 2 x WO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 210.478Å b: 45.778Å c: 130.273Å
α: 90° β: 104.97° γ: 90°
R-values:
R R work R free
0.248 0.248 0.284
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Intrinsically disordered protein.
Dunker et al. (2001)
12 more

4 mentions without citation

The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase.
Cronin et al. (2003)
3 more