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› 4pcp

X-ray diffraction
1.63Å resolution

Crystal structure of Phosphotriesterase variant R0

Released:
DOI: 10.2210/pdb4pcp/pdb
Model geometry
Fit model/data
PDB entry 4pcp coloured by chain, front view.
PDB entry 4pcp coloured by chain, side view.
PDB entry 4pcp coloured by chain, top view.
Source organism: Brevundimonas diminuta
Primary publication:
The role of protein dynamics in the evolution of new enzyme function.
Campbell E, Kaltenbach M, Correy GJ, Carr PD, Porebski BT, Livingstone EK, Afriat-Jurnou L, Buckle AM, Weik M, Hollfelder F, Tokuriki N, Jackson CJ
Nat Chem Biol 12 944-950 (2016)
PMID: 27618189

Function and Biology Details

Reaction catalysed: 
An aryl dialkyl phosphate + H2O = 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-100307 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Parathion hydrolase Chains: A, G
Molecule details ›
Chains: A, G
Length: 333 amino acids
Theoretical weight: 36.06 KDa
Source organism: Brevundimonas diminuta
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A060GYS1 (Residues: 1-333; Coverage: 100%)
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

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

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P21212
Unit cell:
a: 86.141Å b: 86.325Å c: 88.722Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.219
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Conformational dynamics and enzyme evolution.
Petrović et al. (2018)
20 more

5 mentions without citation

A mechanistic view of enzyme evolution.
Yang et al. (2020)
4 more