3ixh
From Proteopedia
(Difference between revisions)
m (Protected "3ixh" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
[[Image:3ixh.png|left|200px]] | [[Image:3ixh.png|left|200px]] | ||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_3ixh", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_3ixh| PDB=3ixh | SCENE= }} | {{STRUCTURE_3ixh| PDB=3ixh | SCENE= }} | ||
===X-ray crystal structure of the extended-spectrum AmpC Y221G mutant beta-lactamase in complex with cefotaxime at 2.3 Angstrom resolution=== | ===X-ray crystal structure of the extended-spectrum AmpC Y221G mutant beta-lactamase in complex with cefotaxime at 2.3 Angstrom resolution=== | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, {{ABSTRACT_PUBMED_19913034}}, adds the Publication Abstract to the page | ||
| - | (as it appears on PubMed at http://www.pubmed.gov), where 19913034 is the PubMed ID number. | ||
| - | --> | ||
{{ABSTRACT_PUBMED_19913034}} | {{ABSTRACT_PUBMED_19913034}} | ||
| Line 22: | Line 11: | ||
==See Also== | ==See Also== | ||
| - | *[[Beta-lactamase]] | + | *[[Beta-lactamase|Beta-lactamase]] |
==Reference== | ==Reference== | ||
Revision as of 07:59, 26 July 2012
Contents |
X-ray crystal structure of the extended-spectrum AmpC Y221G mutant beta-lactamase in complex with cefotaxime at 2.3 Angstrom resolution
Template:ABSTRACT PUBMED 19913034
About this Structure
3ixh is a 2 chain structure of Beta-lactamase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Thomas VL, McReynolds AC, Shoichet BK. Structural bases for stability-function tradeoffs in antibiotic resistance. J Mol Biol. 2010 Feb 12;396(1):47-59. Epub 2009 Nov 10. PMID:19913034 doi:10.1016/j.jmb.2009.11.005
