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4c6b

From Proteopedia

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m (Protected "4c6b" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4c6b| PDB=4c6b | SCENE= }}
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===Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.===
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{{ABSTRACT_PUBMED_24332717}}
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The entry 4c6b is ON HOLD until Paper Publication
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==Function==
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[[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).
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Authors: Ramon-Maiques, S., Lallous, N., Grande-Garcia, A.
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==About this Structure==
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[[4c6b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6B OCA].
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Description: Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.
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==Reference==
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<ref group="xtra">PMID:024332717</ref><references group="xtra"/><references/>
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[[Category: Dihydroorotase]]
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[[Category: Grande-Garcia, A.]]
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[[Category: Lallous, N.]]
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[[Category: Ramon-Maiques, S.]]
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[[Category: Amidohydrolase superfamily]]
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[[Category: De novo pyrimidine biosynthesis]]
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[[Category: Histidinate anion]]
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[[Category: Hydrolase]]
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[[Category: Metalloenzyme]]
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[[Category: Zinc binding]]

Revision as of 11:08, 5 February 2014

Template:STRUCTURE 4c6b

Contents

Crystal structure of the dihydroorotase domain of human CAD with incomplete active site, obtained recombinantly from E. coli.

Template:ABSTRACT PUBMED 24332717

Function

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

About this Structure

4c6b is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • 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

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