1cqe: Difference between revisions
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|PDB= 1cqe |SIZE=350|CAPTION= <scene name='initialview01'>1cqe</scene>, resolution 3.1Å | |PDB= 1cqe |SIZE=350|CAPTION= <scene name='initialview01'>1cqe</scene>, resolution 3.1Å | ||
|SITE= <scene name='pdbsite=COA:Hydrophobic+Channel+Responsible+For+Cycloogenase+Activity'>COA</scene>, <scene name='pdbsite=COB:Hydrophobic+Channel+Responsible+For+Cycloogenase+Activity'>COB</scene>, <scene name='pdbsite=POA:Heme+Pocket+Responsible+For+Peroxidase+Activity'>POA</scene> and <scene name='pdbsite=POB:Heme+Pocket+Responsible+For+Peroxidase+Activity'>POB</scene> | |SITE= <scene name='pdbsite=COA:Hydrophobic+Channel+Responsible+For+Cycloogenase+Activity'>COA</scene>, <scene name='pdbsite=COB:Hydrophobic+Channel+Responsible+For+Cycloogenase+Activity'>COB</scene>, <scene name='pdbsite=POA:Heme+Pocket+Responsible+For+Peroxidase+Activity'>POA</scene> and <scene name='pdbsite=POB:Heme+Pocket+Responsible+For+Peroxidase+Activity'>POB</scene> | ||
|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=FLP:FLURBIPROFEN'>FLP</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Prostaglandin-endoperoxide_synthase Prostaglandin-endoperoxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.1 1.14.99.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Prostaglandin-endoperoxide_synthase Prostaglandin-endoperoxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.1 1.14.99.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqe OCA], [http://www.ebi.ac.uk/pdbsum/1cqe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cqe RCSB]</span> | |||
}} | }} | ||
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[[Category: Mulichak, A M.]] | [[Category: Mulichak, A M.]] | ||
[[Category: Picot, D.]] | [[Category: Picot, D.]] | ||
[[Category: dioxygenase]] | [[Category: dioxygenase]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: peroxidase]] | [[Category: peroxidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:26:30 2008'' | ||
Revision as of 19:26, 30 March 2008
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| , resolution 3.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , , , | ||||||
| Activity: | Prostaglandin-endoperoxide synthase, with EC number 1.14.99.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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