4c6f: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4c6f|  PDB=4c6f  |  SCENE=  }}
===Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 6.5===
{{ABSTRACT_PUBMED_24332717}}


The entry 4c6f is ON HOLD  until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/PYR1_HUMAN PYR1_HUMAN]] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).


Authors: Ramon-Maiques, S., Lallous, N., Grande-Garcia, A.
==About this Structure==
[[4c6f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6F OCA].  


Description: Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 6.5
==Reference==
<ref group="xtra">PMID:024332717</ref><references group="xtra"/><references/>
[[Category: Dihydroorotase]]
[[Category: Grande-Garcia, A.]]
[[Category: Lallous, N.]]
[[Category: Ramon-Maiques, S.]]
[[Category: Amidohydrolase superfamily]]
[[Category: Histidinate anion]]
[[Category: Hydrolase]]
[[Category: Metalloenzyme]]
[[Category: Zinc binding]]

Revision as of 14:18, 5 February 2014

Template:STRUCTURE 4c6f

Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 6.5Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 6.5

Template:ABSTRACT PUBMED 24332717

FunctionFunction

[PYR1_HUMAN] This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).

About this StructureAbout this Structure

4c6f is a 1 chain structure. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Grande-Garcia A, Lallous N, Diaz-Tejada C, Ramon-Maiques S. Structure, Functional Characterization, and Evolution of the Dihydroorotase Domain of Human CAD. Structure. 2013 Dec 10. pii: S0969-2126(13)00428-0. doi:, 10.1016/j.str.2013.10.016. PMID:24332717 doi:http://dx.doi.org/10.1016/j.str.2013.10.016

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OCA