2bww: Difference between revisions

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[[Image:2bww.gif|left|200px]]<br /><applet load="2bww" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2bww.gif|left|200px]]
caption="2bww, resolution 2.61&Aring;" />
 
'''HIS350ALA ESCHERICHIA COLI AMINOPEPTIDASE P'''<br />
{{Structure
|PDB= 2bww |SIZE=350|CAPTION= <scene name='initialview01'>2bww</scene>, resolution 2.61&Aring;
|SITE= <scene name='pdbsite=AC1:Mrd+Binding+Site+For+Chain+A'>AC1</scene>
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene> and <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9]
|GENE=
}}
 
'''HIS350ALA ESCHERICHIA COLI AMINOPEPTIDASE P'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2BWW 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=MN:'>MN</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=FLC:'>FLC</scene> and <scene name='pdbligand=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Known structural/functional Site: <scene name='pdbsite=AC1:Mrd+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BWW OCA].  
2BWW 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=2BWW OCA].  


==Reference==
==Reference==
Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis., Graham SC, Lilley PE, Lee M, Schaeffer PM, Kralicek AV, Dixon NE, Guss JM, Biochemistry. 2006 Jan 24;45(3):964-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16411772 16411772]
Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis., Graham SC, Lilley PE, Lee M, Schaeffer PM, Kralicek AV, Dixon NE, Guss JM, Biochemistry. 2006 Jan 24;45(3):964-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16411772 16411772]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: MN]]
[[Category: MN]]
[[Category: MRD]]
[[Category: MRD]]
[[Category: 'pita-bread' enzyme]]
[[Category: pita-bread enzyme]]
[[Category: aminopeptidase p]]
[[Category: aminopeptidase p]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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[[Category: proline-specific enzyme]]
[[Category: proline-specific enzyme]]


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