2nox: Difference between revisions

Revision as of 21:59, 17 February 2009

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nox.png

Template:STRUCTURE 2nox

Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metalliduransCrystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans

Template:ABSTRACT PUBMED 17198384

About this StructureAbout this Structure

2NOX is a 16 chains structure of sequences from Cupriavidus metallidurans. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE. Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry. 2007 Jan 9;46(1):145-55. PMID:17198384 doi:10.1021/bi0620095

Page seeded by OCA on Tue Feb 17 20:59:11 2009

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE. Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry. 2007 Jan 9;46(1):145-55. PMID:17198384 doi:10.1021/bi0620095

[xtra 1]

@@ Line 20: / Line 20: @@
 ==About this Structure==
-NOX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cupriavidus_metallidurans Cupriavidus metallidurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOX OCA].
+NOX is a 16 chains structure of sequences from [http://en.wikipedia.org/wiki/Cupriavidus_metallidurans Cupriavidus metallidurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOX OCA].
 ==Reference==
-Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis., Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE, Biochemistry. 2007 Jan 9;46(1):145-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17198384 17198384]
+<ref group="xtra">PMID:17198384</ref><references group="xtra"/>
 [[Category: Cupriavidus metallidurans]]
-[[Category: Single protein]]
 [[Category: Tryptophan 2,3-dioxygenase]]
 [[Category: Bale, S.]]
@@ Line 37: / Line 36: @@
 [[Category: Heme protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:59:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:59:11 2009''