1rr9: Difference between revisions

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[[Image:1rr9.jpg|left|200px]]<br /><applet load="1rr9" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1rr9.jpg|left|200px]]
caption="1rr9, resolution 2.1&Aring;" />
 
'''Catalytic domain of E.coli Lon protease'''<br />
{{Structure
|PDB= 1rr9 |SIZE=350|CAPTION= <scene name='initialview01'>1rr9</scene>, resolution 2.1&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53]
|GENE= LON, CAPR, DEG, MUC, LOPA, B0439, C0555 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''Catalytic domain of E.coli Lon protease'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1RR9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RR9 OCA].  
1RR9 is a [[Single protein]] structure of 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=1RR9 OCA].  


==Reference==
==Reference==
The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site., Botos I, Melnikov EE, Cherry S, Tropea JE, Khalatova AG, Rasulova F, Dauter Z, Maurizi MR, Rotanova TV, Wlodawer A, Gustchina A, J Biol Chem. 2004 Feb 27;279(9):8140-8. Epub 2003 Dec 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14665623 14665623]
The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site., Botos I, Melnikov EE, Cherry S, Tropea JE, Khalatova AG, Rasulova F, Dauter Z, Maurizi MR, Rotanova TV, Wlodawer A, Gustchina A, J Biol Chem. 2004 Feb 27;279(9):8140-8. Epub 2003 Dec 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14665623 14665623]
[[Category: Endopeptidase La]]
[[Category: Endopeptidase La]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: SO4]]
[[Category: SO4]]
[[Category: atp-dependent protease]]
[[Category: atp-dependent protease]]
[[Category: catalytic dyad ser-lys]]
[[Category: catalytic dyad ser-ly]]


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