2bwv: Difference between revisions

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[[Image:2bwv.gif|left|200px]]<br /><applet load="2bwv" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2bwv.gif|left|200px]]
caption="2bwv, resolution 1.70&Aring;" />
 
'''HIS361ALA ESCHERICHIA COLI AMINOPEPTIDASE P'''<br />
{{Structure
|PDB= 2bwv |SIZE=350|CAPTION= <scene name='initialview01'>2bwv</scene>, resolution 1.70&Aring;
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene>
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</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=
}}
 
'''HIS361ALA ESCHERICHIA COLI AMINOPEPTIDASE P'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2BWV 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> and <scene name='pdbligand=CL:'>CL</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:Cl+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BWV OCA].  
2BWV 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=2BWV 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: CL]]
[[Category: CL]]
[[Category: MN]]
[[Category: MN]]
[[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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