3frd: Difference between revisions
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m Protected "3frd" [edit=sysop:move=sysop] |
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[[Image:3frd.png|left|200px]] | [[Image:3frd.png|left|200px]] | ||
{{STRUCTURE_3frd| PDB=3frd | SCENE= }} | {{STRUCTURE_3frd| PDB=3frd | SCENE= }} | ||
===S. aureus DHFR complexed with NADPH and folate=== | ===S. aureus DHFR complexed with NADPH and folate=== | ||
{{ABSTRACT_PUBMED_19211577}} | {{ABSTRACT_PUBMED_19211577}} | ||
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==See Also== | ==See Also== | ||
*[[Dihydrofolate reductase]] | *[[Dihydrofolate reductase|Dihydrofolate reductase]] | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:019211577</ref><references group="xtra"/> | ||
[[Category: Dihydrofolate reductase]] | [[Category: Dihydrofolate reductase]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
Revision as of 23:33, 25 July 2012
S. aureus DHFR complexed with NADPH and folate
Template:ABSTRACT PUBMED 19211577
About this Structure
3frd is a 1 chain structure of Dihydrofolate reductase with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
See Also
Reference
- Oefner C, Bandera M, Haldimann A, Laue H, Schulz H, Mukhija S, Parisi S, Weiss L, Lociuro S, Dale GE. Increased hydrophobic interactions of iclaprim with Staphylococcus aureus dihydrofolate reductase are responsible for the increase in affinity and antibacterial activity. J Antimicrob Chemother. 2009 Apr;63(4):687-98. Epub 2009 Feb 11. PMID:19211577 doi:10.1093/jac/dkp024