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1d09

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==About this Structure==
==About this Structure==
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1D09 is a [[Protein complex]] 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].
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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].
==Reference==
==Reference==
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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., Jin L, Stec B, Lipscomb WN, Kantrowitz ER, Proteins. 1999 Dec 1;37(4):729-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10651286 10651286]
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<ref group="xtra">PMID:10651286</ref><references group="xtra"/>
[[Category: Aspartate carbamoyltransferase]]
[[Category: Aspartate carbamoyltransferase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
 
[[Category: Jin, L.]]
[[Category: Jin, L.]]
[[Category: Kantrowitz, E R.]]
[[Category: Kantrowitz, E R.]]
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[[Category: Protein-inhibitor complex aspartate transcarbamoylase aspartate transcarbamylase]]
[[Category: Protein-inhibitor complex aspartate transcarbamoylase aspartate transcarbamylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:55:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:55:36 2009''

Revision as of 15:55, 17 February 2009

Template:STRUCTURE 1d09

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

Template:ABSTRACT PUBMED 10651286

About this Structure

1D09 is a 4 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • 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

Page seeded by OCA on Tue Feb 17 17:55:36 2009

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