1nbi: Difference between revisions

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[[Image:1nbi.png|left|200px]]
[[Image:1nbi.png|left|200px]]


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{{STRUCTURE_1nbi|  PDB=1nbi  |  SCENE=  }}  
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===Structure of R175K mutated glycine N-methyltransferase complexed with S-adenosylmethionine, R175K:SAM.===
===Structure of R175K mutated glycine N-methyltransferase complexed with S-adenosylmethionine, R175K:SAM.===


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{{ABSTRACT_PUBMED_12859184}}
{{ABSTRACT_PUBMED_12859184}}


==About this Structure==
==About this Structure==
1NBI is a 4 chains structure of sequences 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=1NBI OCA].  
[[1nbi]] is a 4 chain structure 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=1NBI OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:12859184</ref><references group="xtra"/>
<ref group="xtra">PMID:012859184</ref><references group="xtra"/>
[[Category: Glycine N-methyltransferase]]
[[Category: Glycine N-methyltransferase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Glycine n-methyltransferase]]
[[Category: Glycine n-methyltransferase]]
[[Category: Methyltransferase]]
[[Category: Methyltransferase]]
 
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:38:07 2009''

Revision as of 19:59, 5 December 2012

File:1nbi.png

Template:STRUCTURE 1nbi

Structure of R175K mutated glycine N-methyltransferase complexed with S-adenosylmethionine, R175K:SAM.

Template:ABSTRACT PUBMED 12859184

About this Structure

1nbi is a 4 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

  1. Takata Y, Huang Y, Komoto J, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F. Catalytic mechanism of glycine N-methyltransferase. Biochemistry. 2003 Jul 22;42(28):8394-402. PMID:12859184 doi:10.1021/bi034245a

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