1e19: Difference between revisions

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[[Image:1e19.gif|left|200px]]<br /><applet load="1e19" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1e19.gif|left|200px]]
caption="1e19, resolution 1.5&Aring;" />
 
'''STRUCTURE OF THE CARBAMATE KINASE-LIKE CARBAMOYL PHOSPHATE SYNTHETASE FROM THE HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS FURIOSUS BOUND TO ADP'''<br />
{{Structure
|PDB= 1e19 |SIZE=350|CAPTION= <scene name='initialview01'>1e19</scene>, resolution 1.5&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Carbamate_kinase Carbamate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.2 2.7.2.2]
|GENE=
}}
 
'''STRUCTURE OF THE CARBAMATE KINASE-LIKE CARBAMOYL PHOSPHATE SYNTHETASE FROM THE HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS FURIOSUS BOUND TO ADP'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1E19 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbamate_kinase Carbamate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.2 2.7.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E19 OCA].  
1E19 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E19 OCA].  


==Reference==
==Reference==
The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases., Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V, J Mol Biol. 2000 Jun 2;299(2):463-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10860751 10860751]
The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases., Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V, J Mol Biol. 2000 Jun 2;299(2):463-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10860751 10860751]
[[Category: Carbamate kinase]]
[[Category: Carbamate kinase]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
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[[Category: adp site]]
[[Category: adp site]]
[[Category: arginine metabolism]]
[[Category: arginine metabolism]]
[[Category: hyperthermophiles]]
[[Category: hyperthermophile]]
[[Category: phosphoryl group transfer]]
[[Category: phosphoryl group transfer]]
[[Category: pyrococcus furiosus]]
[[Category: pyrococcus furiosus]]


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