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):
This entry contains 1 unique UniProt protein: