2e77

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[[Image:2e77.png|left|200px]]
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{{STRUCTURE_2e77| PDB=2e77 | SCENE= }}
{{STRUCTURE_2e77| PDB=2e77 | SCENE= }}
===Crystal structure of L-lactate oxidase with pyruvate complex===
===Crystal structure of L-lactate oxidase with pyruvate complex===
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{{ABSTRACT_PUBMED_17517371}}
{{ABSTRACT_PUBMED_17517371}}
==About this Structure==
==About this Structure==
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2E77 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Aerococcus_viridans Aerococcus viridans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E77 OCA].
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[[2e77]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerococcus_viridans Aerococcus viridans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E77 OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:17517371</ref><references group="xtra"/>
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<ref group="xtra">PMID:017517371</ref><ref group="xtra">PMID:017172470</ref><references group="xtra"/>
[[Category: Aerococcus viridans]]
[[Category: Aerococcus viridans]]
[[Category: Lactate 2-monooxygenase]]
[[Category: Lactate 2-monooxygenase]]
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:22:26 2009''
 

Revision as of 10:35, 6 January 2013

Template:STRUCTURE 2e77

Crystal structure of L-lactate oxidase with pyruvate complex

Template:ABSTRACT PUBMED 17517371

About this Structure

2e77 is a 4 chain structure with sequence from Aerococcus viridans. Full crystallographic information is available from OCA.

Reference

  • Li SJ, Umena Y, Yorita K, Matsuoka T, Kita A, Fukui K, Morimoto Y. Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution. Biochem Biophys Res Commun. 2007 Jul 13;358(4):1002-7. Epub 2007 May 11. PMID:17517371 doi:10.1016/j.bbrc.2007.05.021
  • Doukov TI, Hemmi H, Drennan CL, Ragsdale SW. Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases. J Biol Chem. 2007 Mar 2;282(9):6609-18. Epub 2006 Dec 15. PMID:17172470 doi:http://dx.doi.org/10.1074/jbc.M609828200

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