2g8d

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{{STRUCTURE_2g8d| PDB=2g8d | SCENE= }}
{{STRUCTURE_2g8d| PDB=2g8d | SCENE= }}
===Lactobacillus casei thymidylate synthase Y261W-dUMP complex===
===Lactobacillus casei thymidylate synthase Y261W-dUMP complex===
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{{ABSTRACT_PUBMED_16768437}}
{{ABSTRACT_PUBMED_16768437}}
==About this Structure==
==About this Structure==
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2G8D is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G8D OCA].
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[[2g8d]] is a 1 chain structure of [[Thymidylate synthase]] with sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G8D OCA].
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==See Also==
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*[[Thymidylate synthase|Thymidylate synthase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:16768437</ref><references group="xtra"/>
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<ref group="xtra">PMID:016768437</ref><references group="xtra"/>
[[Category: Lactobacillus casei]]
[[Category: Lactobacillus casei]]
[[Category: Thymidylate synthase]]
[[Category: Thymidylate synthase]]
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[[Category: Dump complex]]
[[Category: Dump complex]]
[[Category: Methyltransferase]]
[[Category: Methyltransferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 05:46:51 2009''
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Revision as of 12:11, 27 July 2012

Template:STRUCTURE 2g8d

Contents

Lactobacillus casei thymidylate synthase Y261W-dUMP complex

Template:ABSTRACT PUBMED 16768437

About this Structure

2g8d is a 1 chain structure of Thymidylate synthase with sequence from Lactobacillus casei. Full crystallographic information is available from OCA.

See Also

Reference

  • Newby Z, Lee TT, Morse RJ, Liu Y, Liu L, Venkatraman P, Santi DV, Finer-Moore JS, Stroud RM. The role of protein dynamics in thymidylate synthase catalysis: variants of conserved 2'-deoxyuridine 5'-monophosphate (dUMP)-binding Tyr-261. Biochemistry. 2006 Jun 20;45(24):7415-28. PMID:16768437 doi:10.1021/bi060152s

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