3any
From Proteopedia
(Difference between revisions)
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- | + | [[Image:3any.jpg|left|200px]] | |
- | The | + | <!-- |
+ | The line below this paragraph, containing "STRUCTURE_3any", creates the "Structure Box" on the page. | ||
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+ | {{STRUCTURE_3any| PDB=3any | SCENE= }} | ||
- | + | ===Crystal structure of ethanolamine ammonia-lyase from escherichia coli complexed with CN-CBL and (R)-2-amino-1-propanol=== | |
- | Description: Crystal structure of ethanolamine ammonia-lyase from escherichia coli complexed with CN-CBL and (R)-2-amino-1-propanol | ||
- | + | <!-- | |
+ | The line below this paragraph, {{ABSTRACT_PUBMED_21142024}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 21142024 is the PubMed ID number. | ||
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+ | {{ABSTRACT_PUBMED_21142024}} | ||
+ | |||
+ | ==About this Structure== | ||
+ | [[3any]] is a 4 chain structure with 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=3ANY OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:021142024</ref><references group="xtra"/> | ||
+ | [[Category: Escherichia coli]] | ||
+ | [[Category: Ethanolamine ammonia-lyase]] | ||
+ | [[Category: Shibata, N.]] | ||
+ | [[Category: Cobalamin]] | ||
+ | [[Category: Cobalt]] | ||
+ | [[Category: Lyase]] | ||
+ | [[Category: Tim barrel]] |
Revision as of 08:46, 3 August 2011
Crystal structure of ethanolamine ammonia-lyase from escherichia coli complexed with CN-CBL and (R)-2-amino-1-propanol
Template:ABSTRACT PUBMED 21142024
About this Structure
3any is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Shibata N, Higuchi Y, Toraya T. How coenzyme B12-dependent ethanolamine ammonia-lyase deals with both enantiomers of 2-amino-1-propanol as substrates: structure-based rationalization. Biochemistry. 2011 Feb 1;50(4):591-8. Epub 2010 Dec 30. PMID:21142024 doi:10.1021/bi101696h