3b1e
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_3b1e| PDB=3b1e | SCENE= }} | {{STRUCTURE_3b1e| PDB=3b1e | SCENE= }} | ||
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===Crystal structure of betaC-S lyase from Streptococcus anginosus in complex with L-serine: alpha-Aminoacrylate form=== | ===Crystal structure of betaC-S lyase from Streptococcus anginosus in complex with L-serine: alpha-Aminoacrylate form=== | ||
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{{ABSTRACT_PUBMED_22674431}} | {{ABSTRACT_PUBMED_22674431}} | ||
==About this Structure== | ==About this Structure== | ||
- | [[3b1e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[3b1e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptococcus_anginosus"_andrewes_and_horder_1906 "streptococcus anginosus" andrewes and horder 1906]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B1E OCA]. |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:022674431</ref>< | + | <ref group="xtra">PMID:022674431</ref><references group="xtra"/><references/> |
+ | [[Category: Streptococcus anginosus andrewes and horder 1906]] | ||
[[Category: Cystathionine beta-lyase]] | [[Category: Cystathionine beta-lyase]] | ||
- | [[Category: Streptococcus anginosus]] | ||
[[Category: Kezuka, Y.]] | [[Category: Kezuka, Y.]] | ||
[[Category: Nonaka, T.]] | [[Category: Nonaka, T.]] | ||
[[Category: Yoshida, Y.]] | [[Category: Yoshida, Y.]] | ||
[[Category: Lyase]] | [[Category: Lyase]] |
Revision as of 05:56, 22 January 2014
Crystal structure of betaC-S lyase from Streptococcus anginosus in complex with L-serine: alpha-Aminoacrylate form
Template:ABSTRACT PUBMED 22674431
About this Structure
3b1e is a 4 chain structure with sequence from "streptococcus_anginosus"_andrewes_and_horder_1906 "streptococcus anginosus" andrewes and horder 1906. Full crystallographic information is available from OCA.
Reference
- Kezuka Y, Yoshida Y, Nonaka T. Structural insights into catalysis by betaC-S lyase from Streptococcus anginosus. Proteins. 2012 Jun 6. doi: 10.1002/prot.24129. PMID:22674431 doi:10.1002/prot.24129