1dq8: Difference between revisions

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==About this Structure==
==About this Structure==
1DQ8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQ8 OCA].  
1DQ8 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQ8 OCA].  


==Reference==
==Reference==
Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis., Istvan ES, Palnitkar M, Buchanan SK, Deisenhofer J, EMBO J. 2000 Mar 1;19(5):819-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10698924 10698924]
<ref group="xtra">PMID:10698924</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Buchanan, S K.]]
[[Category: Buchanan, S K.]]
[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer, J.]]
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:11:02 2009''

Revision as of 05:11, 17 February 2009

File:1dq8.png


PDB ID 1dq8

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1dq8, resolution 2.10Å ()
Ligands: , ,
Activity: Hydroxymethylglutaryl-CoA reductase (NADPH), with EC number 1.1.1.34
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG AND COACOMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG AND COA

Template:ABSTRACT PUBMED 10698924

About this StructureAbout this Structure

1DQ8 is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Istvan ES, Palnitkar M, Buchanan SK, Deisenhofer J. Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. EMBO J. 2000 Mar 1;19(5):819-30. PMID:10698924 doi:10.1093/emboj/19.5.819

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