THREE-DIMENSIONAL STRUCTURE OF THE ZINC-CONTAINING PHOSPHOTRIESTERASE WITH BOUND SUBSTRATE ANALOG TRIETHYLPHOSPHATE
The structure was published by Benning, M.M., Hong, S.B., Raushel, F.M., and Holden, H.M., in 2000 in a paper entitled "The binding of substrate analogs to phosphotriesterase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2000.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of PHOSPHOTRIESTERASE. This molecule has the UniProt identifier P0A434 (OPD_BREDI). The sample contained 331 residues which is 99% of the natural sequence. Out of 331 residues 329 were observed and are deposited in the PDB.
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: