1d09: Difference between revisions

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{{Seed}}
[[Image:1d09.png|left|200px]]
[[Image:1d09.png|left|200px]]


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{{STRUCTURE_1d09|  PDB=1d09  |  SCENE=  }}  
{{STRUCTURE_1d09|  PDB=1d09  |  SCENE=  }}  


===ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)===
===ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)===


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{{ABSTRACT_PUBMED_10651286}}
{{ABSTRACT_PUBMED_10651286}}


==About this Structure==
==About this Structure==
1D09 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D09 OCA].  
[[1d09]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D09 OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:10651286</ref><references group="xtra"/>
<ref group="xtra">PMID:010651286</ref><ref group="xtra">PMID:016120448</ref><references group="xtra"/>
[[Category: Aspartate carbamoyltransferase]]
[[Category: Aspartate carbamoyltransferase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Stec, B.]]
[[Category: Stec, B.]]
[[Category: Protein-inhibitor complex aspartate transcarbamoylase aspartate transcarbamylase]]
[[Category: Protein-inhibitor complex aspartate transcarbamoylase aspartate transcarbamylase]]
 
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:55:36 2009''

Revision as of 20:20, 21 October 2012

File:1d09.png

Template:STRUCTURE 1d09

ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)

Template:ABSTRACT PUBMED 10651286

About this Structure

1d09 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  1. Jin L, Stec B, Lipscomb WN, Kantrowitz ER. Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A. Proteins. 1999 Dec 1;37(4):729-42. PMID:10651286
  2. Stieglitz KA, Dusinberre KJ, Cardia JP, Tsuruta H, Kantrowitz ER. Structure of the E.coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle. J Mol Biol. 2005 Sep 16;352(2):478-86. PMID:16120448 doi:10.1016/j.jmb.2005.07.046

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