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3c2z

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==About this Structure==
==About this Structure==
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3C2Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C2Z OCA].
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3C2Z is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C2Z OCA].
==Reference==
==Reference==
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Crystal structure analysis and in silico pKa calculations suggest strong pKa shifts of ligands as driving force for high-affinity binding to TGT., Ritschel T, Hoertner S, Heine A, Diederich F, Klebe G, Chembiochem. 2009 Mar 2;10(4):716-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19199329 19199329]
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<ref group="xtra">PMID:19199329</ref><references group="xtra"/>
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[[Category: Queuine tRNA-ribosyltransferase]]
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[[Category: Single protein]]
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[[Category: Zymomonas mobilis]]
[[Category: Zymomonas mobilis]]
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[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
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[[Category: TRNA-guanine transglycosylase]]
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[[Category: Heine, A.]]
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[[Category: Klebe, G.]]
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[[Category: Ritschel, T.]]
[[Category: Glycosyltransferase]]
[[Category: Glycosyltransferase]]
[[Category: Metal-binding]]
[[Category: Metal-binding]]
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[[Category: Zinc]]
[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 25 20:36:04 2009''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 11:28:21 2010''

Revision as of 08:19, 22 September 2010

Template:STRUCTURE 3c2z

tRNA-Guanine Transglycosylase (TGT) in complex with 6-Amino-2-[(thiophen-2-ylmethyl)-amino]-1,7-dihydro-imidazo[4,5-g]quinazolin-8-one

Template:ABSTRACT PUBMED 19199329

About this Structure

3C2Z is a 1 chain structure with sequence from Zymomonas mobilis. Full crystallographic information is available from OCA.

Reference

  • Ritschel T, Hoertner S, Heine A, Diederich F, Klebe G. Crystal structure analysis and in silico pKa calculations suggest strong pKa shifts of ligands as driving force for high-affinity binding to TGT. Chembiochem. 2009 Mar 2;10(4):716-27. PMID:19199329 doi:10.1002/cbic.200800782

Page seeded by OCA on Wed Sep 22 11:28:21 2010

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