3bk9: Difference between revisions

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==About this Structure==
==About this Structure==
3BK9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BK9 OCA].  
3BK9 is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BK9 OCA].  


==Reference==
==Reference==
Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding., Thackray SJ, Bruckmann C, Anderson JL, Campbell LP, Xiao R, Zhao L, Mowat CG, Forouhar F, Tong L, Chapman SK, Biochemistry. 2008 Oct 7;47(40):10677-84. Epub 2008 Sep 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18783250 18783250]
<ref group="xtra">PMID:18783250</ref><references group="xtra"/>
[[Category: Single protein]]
[[Category: Tryptophan 2,3-dioxygenase]]
[[Category: Tryptophan 2,3-dioxygenase]]
[[Category: Xanthomonas campestris pv. campestris]]
[[Category: Xanthomonas campestris pv. campestris]]
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[[Category: Tryptophan dioxygenase]]
[[Category: Tryptophan dioxygenase]]


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Revision as of 02:56, 17 February 2009

File:3bk9.png

Template:STRUCTURE 3bk9

H55A mutant of tryptophan 2,3-dioxygenase from Xanthomonas campestrisH55A mutant of tryptophan 2,3-dioxygenase from Xanthomonas campestris

Template:ABSTRACT PUBMED 18783250

About this StructureAbout this Structure

3BK9 is a 8 chains structure of sequences from Xanthomonas campestris pv. campestris. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Thackray SJ, Bruckmann C, Anderson JL, Campbell LP, Xiao R, Zhao L, Mowat CG, Forouhar F, Tong L, Chapman SK. Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding. Biochemistry. 2008 Oct 7;47(40):10677-84. Epub 2008 Sep 11. PMID:18783250 doi:10.1021/bi801202a

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