1hv9: Difference between revisions
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[[Image:1hv9.png|left|200px]] | [[Image:1hv9.png|left|200px]] | ||
{{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=== | ||
{{ABSTRACT_PUBMED_11329257}} | {{ABSTRACT_PUBMED_11329257}} | ||
==About this Structure== | ==About this Structure== | ||
[[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== | ||
<ref group="xtra">PMID: | <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]] | ||
| Line 29: | Line 17: | ||
[[Category: Roderick, S L.]] | [[Category: Roderick, S L.]] | ||
[[Category: Left-handed parallel beta-helix]] | [[Category: Left-handed parallel beta-helix]] | ||
[[Category: Transferase]] | |||
Revision as of 18:55, 21 November 2012
STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITESSTRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES
Template:ABSTRACT PUBMED 11329257
About this StructureAbout this Structure
1hv9 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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