3dl6

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{{STRUCTURE_3dl6| PDB=3dl6 | SCENE= }}
{{STRUCTURE_3dl6| PDB=3dl6 | SCENE= }}
===Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis===
===Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis===
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{{ABSTRACT_PUBMED_18672899}}
{{ABSTRACT_PUBMED_18672899}}
==About this Structure==
==About this Structure==
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3DL6 is a 5 chains structure of sequences from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA].
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[[3dl6]] is a 5 chain structure of [[Dihydrofolate reductase]] and [[Thymidylate synthase]] with sequence from [http://en.wikipedia.org/wiki/Cryptosporidium_hominis Cryptosporidium hominis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL6 OCA].
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==See Also==
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*[[Dihydrofolate reductase|Dihydrofolate reductase]]
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*[[Thymidylate synthase|Thymidylate synthase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:18672899</ref><references group="xtra"/>
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<ref group="xtra">PMID:018672899</ref><references group="xtra"/>
[[Category: Cryptosporidium hominis]]
[[Category: Cryptosporidium hominis]]
[[Category: Dihydrofolate reductase]]
[[Category: Dihydrofolate reductase]]
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[[Category: Enzyme-ligand complex]]
[[Category: Enzyme-ligand complex]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:53:37 2009''
 

Revision as of 16:21, 27 July 2012

Template:STRUCTURE 3dl6

Contents

Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR from Cryptosporidium hominis

Template:ABSTRACT PUBMED 18672899

About this Structure

3dl6 is a 5 chain structure of Dihydrofolate reductase and Thymidylate synthase with sequence from Cryptosporidium hominis. Full crystallographic information is available from OCA.

See Also

Reference

  • Martucci WE, Vargo MA, Anderson KS. Explaining an unusually fast parasitic enzyme: folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase. Biochemistry. 2008 Aug 26;47(34):8902-11. Epub 2008 Aug 2. PMID:18672899 doi:10.1021/bi800466z

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