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1tvc

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[[Image:1tvc.png|left|200px]]
[[Image:1tvc.png|left|200px]]
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{{STRUCTURE_1tvc| PDB=1tvc | SCENE= }}
{{STRUCTURE_1tvc| PDB=1tvc | SCENE= }}
===FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)===
===FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)===
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{{ABSTRACT_PUBMED_15379538}}
{{ABSTRACT_PUBMED_15379538}}
==About this Structure==
==About this Structure==
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1TVC is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVC OCA].
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[[1tvc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVC OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:15379538</ref><references group="xtra"/>
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<ref group="xtra">PMID:015379538</ref><references group="xtra"/>
[[Category: Methane monooxygenase]]
[[Category: Methane monooxygenase]]
[[Category: Methylococcus capsulatus]]
[[Category: Methylococcus capsulatus]]
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[[Category: Fad-binding]]
[[Category: Fad-binding]]
[[Category: Nadh-binding]]
[[Category: Nadh-binding]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:59:29 2009''
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Revision as of 13:47, 5 January 2013

Template:STRUCTURE 1tvc

FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)

Template:ABSTRACT PUBMED 15379538

About this Structure

1tvc is a 1 chain structure with sequence from Methylococcus capsulatus. Full experimental information is available from OCA.

Reference

  • Chatwood LL, Muller J, Gross JD, Wagner G, Lippard SJ. NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath). Biochemistry. 2004 Sep 28;43(38):11983-91. PMID:15379538 doi:10.1021/bi049066n

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