3at1
From Proteopedia
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===CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH=== | ===CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH=== | ||
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{{ABSTRACT_PUBMED_2405902}} | {{ABSTRACT_PUBMED_2405902}} | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[3at1]] 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=3AT1 OCA]. | |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:002405902</ref><ref group="xtra">PMID:016120448</ref><references group="xtra"/> |
[[Category: Aspartate carbamoyltransferase]] | [[Category: Aspartate carbamoyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Gouaux, J E.]] | [[Category: Gouaux, J E.]] | ||
[[Category: Lipscomb, W N.]] | [[Category: Lipscomb, W N.]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 03:47:37 2009'' |
Revision as of 22:59, 7 January 2013
CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH
Template:ABSTRACT PUBMED 2405902
About this Structure
3at1 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Gouaux JE, Lipscomb WN. Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-A resolution and neutral pH. Biochemistry. 1990 Jan 16;29(2):389-402. PMID:2405902
- 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