3frd
From Proteopedia
(Difference between revisions)
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| - | [[Image:3frd.png|left|200px]] | ||
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{{STRUCTURE_3frd| PDB=3frd | SCENE= }} | {{STRUCTURE_3frd| PDB=3frd | SCENE= }} | ||
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===S. aureus DHFR complexed with NADPH and folate=== | ===S. aureus DHFR complexed with NADPH and folate=== | ||
| + | {{ABSTRACT_PUBMED_19211577}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/DYR_STAAU DYR_STAAU]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | ||
==About this Structure== | ==About this Structure== | ||
| - | [[3frd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[3frd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FRD OCA]. |
==See Also== | ==See Also== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:019211577</ref><references group="xtra"/> | + | <ref group="xtra">PMID:019211577</ref><references group="xtra"/><references/> |
[[Category: Dihydrofolate reductase]] | [[Category: Dihydrofolate reductase]] | ||
| - | [[Category: Staphylococcus aureus]] | ||
[[Category: Dale-Glenn, E.]] | [[Category: Dale-Glenn, E.]] | ||
[[Category: Oefner, C.]] | [[Category: Oefner, C.]] | ||
Revision as of 11:56, 20 November 2013
Contents |
S. aureus DHFR complexed with NADPH and folate
Template:ABSTRACT PUBMED 19211577
Function
[DYR_STAAU] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
About this Structure
3frd is a 1 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. 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
