› 3cs2

X-ray diffraction
1.95Å resolution

Crystal structure of PTE G60A mutant

Released:
DOI: 10.2210/pdb3cs2/pdb
Model geometry
Fit model/data
PDB entry 3cs2 coloured by chain, front view.
PDB entry 3cs2 coloured by chain, side view.
PDB entry 3cs2 coloured by chain, top view.
Source organism: Brevundimonas diminuta
Primary publication:
Structure of diethyl phosphate bound to the binuclear metal center of phosphotriesterase.
Kim J, Tsai PC, Chen SL, Himo F, Almo SC, Raushel FM
Biochemistry 47 9497-504 (2008)
PMID: 18702530

Function and Biology Details

Reaction catalysed: 
An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141251 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Parathion hydrolase Chains: A, B, K, P
Molecule details ›
Chains: A, B, K, P
Length: 331 amino acids
Theoretical weight: 35.94 KDa
Source organism: Brevundimonas diminuta
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A434 (Residues: 34-364; Coverage: 99%)
Gene name: opd
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

2 bound ligands:
Ligand CAC 4 x CAC
Ligand CO 8 x CO
1 modified residue:
Ligand KCX 4 x KCX

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X3A
Spacegroup: P1
Unit cell:
a: 55.295Å b: 68.299Å c: 90.03Å
α: 90.05° β: 100.42° γ: 89.96°
R-values:
R R work R free
0.17 0.167 0.224
Expression system: Escherichia coli

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Citations

5 review citations

Progress in ab initio QM/MM free-energy simulations of electrostatic energies in proteins: accelerated QM/MM studies of pKa, redox reactions and solvation free energies.
Kamerlin et al. (2009)
4 more

1 mention without citation

Structural determinants for the stereoselective hydrolysis of chiral substrates by phosphotriesterase.
Tsai et al. (2010)