1pd2

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[[Image:1pd2.gif|left|200px]]<br /><applet load="1pd2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pd2.gif|left|200px]]
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caption="1pd2, resolution 2.3&Aring;" />
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'''CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE'''<br />
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{{Structure
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|PDB= 1pd2 |SIZE=350|CAPTION= <scene name='initialview01'>1pd2</scene>, resolution 2.3&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Prostaglandin-D_synthase Prostaglandin-D synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.99.2 5.3.99.2]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1PD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=GTT:'>GTT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Prostaglandin-D_synthase Prostaglandin-D synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.99.2 5.3.99.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PD2 OCA].
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1PD2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PD2 OCA].
==Reference==
==Reference==
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Cloning and crystal structure of hematopoietic prostaglandin D synthase., Kanaoka Y, Ago H, Inagaki E, Nanayama T, Miyano M, Kikuno R, Fujii Y, Eguchi N, Toh H, Urade Y, Hayaishi O, Cell. 1997 Sep 19;90(6):1085-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9323136 9323136]
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Cloning and crystal structure of hematopoietic prostaglandin D synthase., Kanaoka Y, Ago H, Inagaki E, Nanayama T, Miyano M, Kikuno R, Fujii Y, Eguchi N, Toh H, Urade Y, Hayaishi O, Cell. 1997 Sep 19;90(6):1085-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9323136 9323136]
[[Category: Prostaglandin-D synthase]]
[[Category: Prostaglandin-D synthase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: gst]]
[[Category: gst]]
[[Category: hematopoietic prostaglandin d synthase]]
[[Category: hematopoietic prostaglandin d synthase]]
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[[Category: pgds]]
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[[Category: pgd]]
[[Category: sigma-class gst]]
[[Category: sigma-class gst]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:51 2008''

Revision as of 11:22, 20 March 2008


PDB ID 1pd2

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands:
Activity: Prostaglandin-D synthase, with EC number 5.3.99.2
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE


Overview

Hematopoietic prostaglandin (PG) D synthase is the key enzyme for production of the D and J series of prostanoids in the immune system and mast cells. We isolated a cDNA for the rat enzyme, crystallized the recombinant enzyme, and determined the three-dimensional structure of the enzyme complexed with glutathione at 2.3 A resolution. The enzyme is the first member of the sigma class glutathione S-transferase (GST) from vertebrates and possesses a prominent cleft as the active site, which is never seen among other members of the GST family. The unique 3-D architecture of the cleft leads to the putative substrate binding mode and its catalytic mechanism, responsible for the specific isomerization from PGH2 to PGD2.

About this Structure

1PD2 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Cloning and crystal structure of hematopoietic prostaglandin D synthase., Kanaoka Y, Ago H, Inagaki E, Nanayama T, Miyano M, Kikuno R, Fujii Y, Eguchi N, Toh H, Urade Y, Hayaishi O, Cell. 1997 Sep 19;90(6):1085-95. PMID:9323136

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