1gup: Difference between revisions

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[[Image:1gup.png|left|200px]]
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===STRUCTURE OF NUCLEOTIDYLTRANSFERASE COMPLEXED WITH UDP-GALACTOSE===
===STRUCTURE OF NUCLEOTIDYLTRANSFERASE COMPLEXED WITH UDP-GALACTOSE===


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{{ABSTRACT_PUBMED_9063869}}


==About this Structure==
==About this Structure==
1GUP is a 4 chains structure of sequences 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=1GUP OCA].  
[[1gup]] 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=1GUP OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:9063869</ref><references group="xtra"/>
<ref group="xtra">PMID:009063869</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: UTP--hexose-1-phosphate uridylyltransferase]]
[[Category: UTP--hexose-1-phosphate uridylyltransferase]]
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[[Category: Nucleotidyltransferase]]
[[Category: Nucleotidyltransferase]]
[[Category: Transferase]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:15:17 2009''

Revision as of 18:51, 21 November 2012

File:1gup.png

Template:STRUCTURE 1gup

STRUCTURE OF NUCLEOTIDYLTRANSFERASE COMPLEXED WITH UDP-GALACTOSESTRUCTURE OF NUCLEOTIDYLTRANSFERASE COMPLEXED WITH UDP-GALACTOSE

Template:ABSTRACT PUBMED 9063869

About this StructureAbout this Structure

1gup is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Thoden JB, Ruzicka FJ, Frey PA, Rayment I, Holden HM. Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site. Biochemistry. 1997 Feb 11;36(6):1212-22. PMID:9063869 doi:10.1021/bi9626517

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