Crystal Structure of Arachidonic Acid Bound to a Mutant of Prostagladin H Synthase-1 that Forms Predominantly 11-HPETE.
The structure was published by Harman, C.A., Rieke, C.J., Garavito, R.M., and Smith, W.L., in 2004 in a paper entitled "Crystal structure of arachidonic Acid bound to a mutant of prostaglandin endoperoxide h synthase-1 that forms predominantly 11-hydroperoxyeicosatetraenoic Acid." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 3.1 Å and deposited in 2004.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Prostaglandin G/H synthase 1 precursor. This molecule has the UniProt identifier P05979 (PGH1_SHEEP). The sample contained 600 residues which is < 90% of the natural sequence. Out of 600 residues 532 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: