1dt6: Difference between revisions

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[[Image:1dt6.jpg|left|200px]]<br /><applet load="1dt6" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1dt6.jpg|left|200px]]
caption="1dt6, resolution 3.0&Aring;" />
 
'''STRUCTURE OF MAMMALIAN CYTOCHROME P450 2C5'''<br />
{{Structure
|PDB= 1dt6 |SIZE=350|CAPTION= <scene name='initialview01'>1dt6</scene>, resolution 3.0&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1]
|GENE=
}}
 
'''STRUCTURE OF MAMMALIAN CYTOCHROME P450 2C5'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1DT6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=SM:'>SM</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DT6 OCA].  
1DT6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DT6 OCA].  


==Reference==
==Reference==
Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity., Williams PA, Cosme J, Sridhar V, Johnson EF, McRee DE, Mol Cell. 2000 Jan;5(1):121-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10678174 10678174]
Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity., Williams PA, Cosme J, Sridhar V, Johnson EF, McRee DE, Mol Cell. 2000 Jan;5(1):121-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10678174 10678174]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: progesterone 21-hydroxylase]]
[[Category: progesterone 21-hydroxylase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:15 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:01 2008''

Revision as of 11:44, 20 March 2008

File:1dt6.jpg


PDB ID 1dt6

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands: , and
Activity: Unspecific monooxygenase, with EC number 1.14.14.1
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF MAMMALIAN CYTOCHROME P450 2C5


OverviewOverview

Microsomal cytochrome P450s participate in xenobiotic detoxification, procarcinogen activation, and steroid hormone synthesis. The first structure of a mammalian microsomal P450 suggests that the association of P450s with the endoplasmic reticulum involves a hydrophobic surface of the protein formed by noncontiguous portions of the polypeptide chain. This interaction places the entrance of the putative substrate access channel in or near the membrane and orients the face of the protein proximal to the heme cofactor perpendicular to the plane of the membrane for interaction with the P450 reductase. This structure offers a template for modeling other mammalian P450s and should aid drug discovery and the prediction of drug-drug interactions.

About this StructureAbout this Structure

1DT6 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity., Williams PA, Cosme J, Sridhar V, Johnson EF, McRee DE, Mol Cell. 2000 Jan;5(1):121-31. PMID:10678174

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