1d09
From Proteopedia
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[[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 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: | + | <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]] | |
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Revision as of 20:20, 21 October 2012
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
- 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
- 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