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1prh
From Proteopedia
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|PDB= 1prh |SIZE=350|CAPTION= <scene name='initialview01'>1prh</scene>, resolution 3.5Å | |PDB= 1prh |SIZE=350|CAPTION= <scene name='initialview01'>1prh</scene>, resolution 3.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1prh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prh OCA], [http://www.ebi.ac.uk/pdbsum/1prh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1prh RCSB]</span> | ||
}} | }} | ||
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[[Category: Loll, P J.]] | [[Category: Loll, P J.]] | ||
[[Category: Picot, D.]] | [[Category: Picot, D.]] | ||
| - | [[Category: HEM]] | ||
[[Category: oxidoreductase(dioxygenase]] | [[Category: oxidoreductase(dioxygenase]] | ||
[[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 23:03:37 2008'' |
Revision as of 20:03, 30 March 2008
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| , resolution 3.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN PROSTAGLANDIN H2 SYNTHASE-1
Overview
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 Structure
1PRH is a Single protein structure of sequence from Ovis aries. The following page contains interesting information on the relation of 1PRH with [Cyclooxygenase]. Full crystallographic information is available from OCA.
Reference
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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