1yqs: Difference between revisions
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[[Image:1yqs.png|left|200px]] | [[Image:1yqs.png|left|200px]] | ||
{{STRUCTURE_1yqs| PDB=1yqs | SCENE= }} | {{STRUCTURE_1yqs| PDB=1yqs | SCENE= }} | ||
===Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam=== | ===Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam=== | ||
{{ABSTRACT_PUBMED_15909988}} | {{ABSTRACT_PUBMED_15909988}} | ||
==About this Structure== | ==About this Structure== | ||
[[1yqs]] is a 1 chain structure of [[Carboxypeptidase]] and [[Penicillin-binding protein]] with 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=1YQS OCA]. | |||
==See Also== | |||
*[[Carboxypeptidase|Carboxypeptidase]] | |||
*[[Penicillin-binding protein|Penicillin-binding protein]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:015909988</ref><references group="xtra"/> | ||
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | ||
[[Category: Streptomyces sp.]] | [[Category: Streptomyces sp.]] | ||
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[[Category: Beta-sultam]] | [[Category: Beta-sultam]] | ||
[[Category: Cell well biosynthesis]] | [[Category: Cell well biosynthesis]] | ||
[[Category: Hydrolase]] | |||
[[Category: Peptidase]] | [[Category: Peptidase]] | ||
[[Category: Sulfonylation]] | [[Category: Sulfonylation]] | ||
Revision as of 00:57, 27 July 2012
Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam
Template:ABSTRACT PUBMED 15909988
About this Structure
1yqs is a 1 chain structure of Carboxypeptidase and Penicillin-binding protein with sequence from Streptomyces sp.. Full crystallographic information is available from OCA.
See Also
Reference
- Llinas A, Ahmed N, Cordaro M, Laws AP, Frere JM, Delmarcelle M, Silvaggi NR, Kelly JA, Page MI. Inactivation of bacterial DD-peptidase by beta-sultams. Biochemistry. 2005 May 31;44(21):7738-46. PMID:15909988 doi:https://dx.doi.org/10.1021/bi050110o