1qw7 Summary


Structure of an Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds

The structure was published by Grimsley, J.K., Calamini, B., Wild, J.R., and Mesecar, A.D., in 2005 in a paper entitled "Structural and mutational studies of organophosphorus hydrolase reveal a cryptic and functional allosteric-binding site." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2003.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Parathion hydrolase.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Parathion hydrolase P0A434 (30-365) (OPD_BREDI)search Brevundimonas diminutasearch 97% 336 100%
B Parathion hydrolase P0A434 (30-365) (OPD_BREDI)search Brevundimonas diminutasearch 97% 336 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0A434 (30 - 365) Parathion hydrolase Brevundimonas diminuta

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P0A434) Phosphotriesterase-likesearch Metal-dependent hydrolasessearch PF02126: Phosphotriesterase familysearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P0A434) hydrolase activity, acting on ester bondssearch zinc ion bindingsearch aryldialkylphosphatase activitysearch metal ion bindingsearch hydrolase activitysearch catabolic processsearch dephosphorylationsearch plasma membranesearch membranesearch

Chain InterPro annotation
A, B Aryldialkylphosphatasesearch Aryldialkylphosphatase, zinc-binding sitesearch