1ceg: Difference between revisions

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[[Image:1ceg.gif|left|200px]]<br /><applet load="1ceg" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ceg.gif|left|200px]]
caption="1ceg, resolution 1.80&Aring;" />
 
'''CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE'''<br />
{{Structure
|PDB= 1ceg |SIZE=350|CAPTION= <scene name='initialview01'>1ceg</scene>, resolution 1.80&Aring;
|SITE= <scene name='pdbsite=ACT:Those+For+S.+R61+Are+Listed+Below'>ACT</scene>
|LIGAND= <scene name='pdbligand=CEP:CEPHALOTHIN GROUP'>CEP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4]
|GENE=
}}
 
'''CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1CEG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with <scene name='pdbligand=CEP:'>CEP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] Known structural/functional Site: <scene name='pdbsite=ACT:Those+For+S.+R61+Are+Listed+Below'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEG OCA].  
1CEG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEG OCA].  


==Reference==
==Reference==
Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases., Kuzin AP, Liu H, Kelly JA, Knox JR, Biochemistry. 1995 Jul 25;34(29):9532-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7626623 7626623]
Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases., Kuzin AP, Liu H, Kelly JA, Knox JR, Biochemistry. 1995 Jul 25;34(29):9532-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7626623 7626623]
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: penicillin target]]
[[Category: penicillin target]]


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