1hv9

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[[Image:1hv9.png|left|200px]]
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{{STRUCTURE_1hv9| PDB=1hv9 | SCENE= }}
{{STRUCTURE_1hv9| PDB=1hv9 | SCENE= }}
===STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES===
===STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES===
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{{ABSTRACT_PUBMED_11329257}}
{{ABSTRACT_PUBMED_11329257}}
==About this Structure==
==About this Structure==
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1HV9 is a 2 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=1HV9 OCA].
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[[1hv9]] is a 2 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=1HV9 OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:11329257</ref><references group="xtra"/>
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<ref group="xtra">PMID:011329257</ref><ref group="xtra">PMID:011880627</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: UDP-N-acetylglucosamine diphosphorylase]]
[[Category: UDP-N-acetylglucosamine diphosphorylase]]
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[[Category: Roderick, S L.]]
[[Category: Roderick, S L.]]
[[Category: Left-handed parallel beta-helix]]
[[Category: Left-handed parallel beta-helix]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:44:39 2009''
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Revision as of 15:55, 21 November 2012

Template:STRUCTURE 1hv9

STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES

Template:ABSTRACT PUBMED 11329257

About this Structure

1hv9 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Olsen LR, Roderick SL. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry. 2001 Feb 20;40(7):1913-21. PMID:11329257
  • Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. PMID:11880627 doi:10.1073/pnas.052706099

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