1ml4: Difference between revisions

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[[Image:1ml4.gif|left|200px]]<br /><applet load="1ml4" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ml4.gif|left|200px]]
caption="1ml4, resolution 1.8&Aring;" />
 
'''The PALA-liganded Aspartate transcarbamoylase catalytic subunit from Pyrococcus abyssi'''<br />
{{Structure
|PDB= 1ml4 |SIZE=350|CAPTION= <scene name='initialview01'>1ml4</scene>, resolution 1.8&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC ACID'>PAL</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2]
|GENE= PyrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 Pyrococcus abyssi])
}}
 
'''The PALA-liganded Aspartate transcarbamoylase catalytic subunit from Pyrococcus abyssi'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1ML4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with <scene name='pdbligand=PAL:'>PAL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ML4 OCA].  
1ML4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ML4 OCA].  


==Reference==
==Reference==
Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate., Van Boxstael S, Cunin R, Khan S, Maes D, J Mol Biol. 2003 Feb 7;326(1):203-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12547202 12547202]
Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate., Van Boxstael S, Cunin R, Khan S, Maes D, J Mol Biol. 2003 Feb 7;326(1):203-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12547202 12547202]
[[Category: Aspartate carbamoyltransferase]]
[[Category: Aspartate carbamoyltransferase]]
[[Category: Pyrococcus abyssi]]
[[Category: Pyrococcus abyssi]]
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[[Category: protein inhibitor complex]]
[[Category: protein inhibitor complex]]


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