1cqe
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PROSTAGLANDIN H2 SYNTHASE-1 COMPLEX WITH FLURBIPROFEN
OverviewOverview
The three-dimensional structure of prostaglandin H2 synthase-1, an, integral membrane protein, has been determined at 3.5 A resolution by, X-ray crystallography. This bifunctional enzyme comprises three, independent folding units: an epidermal growth factor domain, a, membrane-binding motif and an enzymatic domain. Two adjacent but spatially, distinct active sites were found for its haem-dependent peroxidase and, cyclooxygenase activities. The cyclooxygenase active site is created by a, long, hydrophobic channel that is the site of non-steroidal, anti-inflammatory drug binding. The conformation of the membrane-binding, motif strongly suggests that the enzyme integrates into only one leaflet, of the lipid bilayer and is thus a monotopic membrane protein.
About this StructureAbout this Structure
1CQE is a [Single protein] structure of sequence from [Ovis aries] with BOG, HEM and FLP as [ligands]. Active as [Prostaglandin-endoperoxide synthase], with EC number [1.14.99.1]. Structure known Active Sites: COA, COB, POA and POB. Full crystallographic information is available from [OCA].
ReferenceReference
The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1., Picot D, Loll PJ, Garavito RM, Nature. 1994 Jan 20;367(6460):243-9. PMID:8121489
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