Protein Information

General Information
MoonProt ID131
First appeared in release1.0
Name(s)Prostaglandin H2 Synthase Prostaglandin G/H synthase 1 Cyclooxygenase-1 Prostaglandin-endoperoxide synthase 1 COX-1 COX1 Prostaglandin H2 synthase 1 PGH synthase 1 PGHS-1 PHS 1 Prostaglandin-endoperoxide synthase 1 Gene Name: PTGS1
UniProt IDP05979 (PGH1_SHEEP) Reviewed
GO termsGO:0001516 prostaglandin biosynthetic process GO:0006629 lipid metabolic process GO:0006631 fatty acid metabolic process GO:0006633 fatty acid biosynthetic process GO:0006693 prostaglandin metabolic process GO:0006979 response to oxidative stress GO:0008217 regulation of blood pressure GO:0055114 oxidation-reduction process GO:0004601 peroxidase activity GO:0004666 prostaglandin-endoperoxide synthase activity GO:0016491 oxidoreductase activity GO:0020037 heme binding GO:0046872 metal ion binding GO:0051213 dioxygenase activity GO:0005634 nucleus GO:0005737 cytoplasm GO:0005783 endoplasmic reticulum GO:0005789 endoplasmic reticulum membrane GO:0016020 membrane GO:0016021 integral component of membrane GO:0031090 organelle membrane GO:0043231 intracellular membrane-bounded organelle GO:0004601 peroxidase activity
Organisms for which functions have been demonstratedOvis aries (Sheep)
Sequence length600
FASTA sequence>sp|P05979|PGH1_SHEEP Prostaglandin G/H synthase 1 OS=Ovis aries GN=PTGS1 PE=1 SV=3 MSRQSISLRFPLLLLLLSPSPVFSADPGAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTTLRPSPSFIHFMLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQTARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDVIKESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLNTKTCPYVSFHVPDPRQEDRPGVERPPTEL"
Structure Information
PDB ID1HT8, 2OYU, 1CQE, 1EQG, 1EQH, 1PGF, 1PGG, 1FE2, 1IGZ, 1IGX, 1PGE, 1PTH, 1Q4G, 2AYL, 3KK6, 3N8V, 3N8W, 3N8X, 3N8Y, 3N8Z, 2OYE, 1PRH, 1HT5, 1U67, 1PTH, 1DIY, 3N8Y, 3N8W, 1PRH, 1HT5, 1EBV
Quaternary structure
Function 1
Function descriptionProstaglandin H2 synthase-1, enzyme Arachidonate + AH(2) + 2 O(2) <=> prostaglandin H(2) + A + H(2)O Lipid metabolism, prostaglandin biosynthesis
References for functionPicot D, Loll PJ, Garavito RM. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature. 1994 Jan 20. PMID: 8121489
E.C. number1.14.99.1
Location of functional site(s)Active site:207,385 Metal binding site:388 Other functional site:530,104
Cellular location of functionEndoplasmic Reticulum membrane, transmembrane protein
Comments
Function 2
Function descriptionPeroxidase and cyclo-oxygenase 2 phenolic donor + H(2)O(2) <=> 2 phenoxyl radical of the donor + 2 H(2)O
References for functionSelinsky BS, Gupta K, Sharkey CT, Loll PJ. Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations. Biochemistry. 2001 May 1. PMID: 11318639
E.C. number1.11.1.7
Location of functional site(s)
Cellular location of functionCytoplasm
CommentsActive site containing Tyr385, Tyr355, Ser530, Glu524, Arg120 interactions. Synthesis and use of iodinated nonsteroidal antiinflammatory drug analogs as crystallographic probes of the prostaglandin H2 synthase cyclooxygenase active site. Loll PJ, Picot D, Ekabo O, Garavito RM. Biochemistry. 1996 Jun 11;35(23):7330-40. PMID: 8652509 Active site containg Arg277, Gln358, Arg120, Ile -523, Tyr355 play roles in the inhibition activity. Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations. Selinsky BS, Gupta K, Sharkey CT, Loll PJ. Biochemistry. 2001 May 1;40(17):5172-80. PMID: 11318639