› 1pta

X-ray diffraction
2.1Å resolution

THREE-DIMENSIONAL STRUCTURE OF PHOSPHOTRIESTERASE: AN ENZYME CAPABLE OF DETOXIFYING ORGANOPHOSPHATE NERVE AGENTS

Released:
DOI: 10.2210/pdb1pta/pdb
PDB entry 1pta coloured by chain, front view.
PDB entry 1pta coloured by chain, side view.
PDB entry 1pta coloured by chain, top view.
Source organism: Brevundimonas diminuta
Primary publication:
Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents.
Benning MM, Kuo JM, Raushel FM, Holden HM
Biochemistry 33 15001-7 (1994)
PMID: 7999757

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 domain:

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 Chain: A
Molecule details ›
Chain: A
Length: 327 amino acids
Theoretical weight: 35.49 KDa
Source organism: Brevundimonas diminuta
UniProt:
  • Canonical: P0A434 (Residues: 36-362; Coverage: 97%)
Gene name: opd
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 80.2Å b: 93.7Å c: 45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 not available not available

Quick links

Citations

16 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
15 more

7 mentions without citation

Bacterial Membrane Vesicles for In Vitro Catalysis.
Thakur et al. (2023)
6 more