1amo
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
- | + | [[1amo]] is a 2 chain structure of [[NADPH-Cytochrome P450 Reductase]] with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMO OCA]. | |
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+ | ==See Also== | ||
+ | *[[NADPH-Cytochrome P450 Reductase]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:009237990</ref><ref group="xtra">PMID:010338023</ref><ref group="xtra">PMID:018980384</ref><references group="xtra"/> |
[[Category: NADPH--hemoprotein reductase]] | [[Category: NADPH--hemoprotein reductase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: X-ray crystallography]] | [[Category: X-ray crystallography]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:40:31 2009'' |
Revision as of 12:51, 28 April 2011
Contents |
THREE-DIMENSIONAL STRUCTURE OF NADPH-CYTOCHROME P450 REDUCTASE: PROTOTYPE FOR FMN-AND FAD-CONTAINING ENZYMES
Template:ABSTRACT PUBMED 9237990
About this Structure
1amo is a 2 chain structure of NADPH-Cytochrome P450 Reductase with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
See Also
Reference
- Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ. Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8411-6. PMID:9237990
- Ayers DJ, Gooley PR, Widmer-Cooper A, Torda AE. Enhanced protein fold recognition using secondary structure information from NMR. Protein Sci. 1999 May;8(5):1127-33. PMID:10338023 doi:10.1110/ps.8.5.1127
- Gherasim CG, Zaman U, Raza A, Banerjee R. Impeded electron transfer from a pathogenic FMN domain mutant of methionine synthase reductase and its responsiveness to flavin supplementation. Biochemistry. 2008 Nov 25;47(47):12515-22. PMID:18980384 doi:10.1021/bi8008328