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4hhe

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{{STRUCTURE_4hhe| PDB=4hhe | SCENE= }}
{{STRUCTURE_4hhe| PDB=4hhe | SCENE= }}
===Quinolinate synthase from Pyrococcus furiosus===
===Quinolinate synthase from Pyrococcus furiosus===
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{{ABSTRACT_PUBMED_23999292}}
==Function==
==Function==
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==About this Structure==
==About this Structure==
[[4hhe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2qs0 2qs0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HHE OCA].
[[4hhe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2qs0 2qs0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HHE OCA].
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==Reference==
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<ref group="xtra">PMID:023999292</ref><references group="xtra"/><references/>
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Quinolinate synthase]]
[[Category: Quinolinate synthase]]

Revision as of 02:43, 20 September 2013

Template:STRUCTURE 4hhe

Contents

Quinolinate synthase from Pyrococcus furiosus

Template:ABSTRACT PUBMED 23999292

Function

[NADA_PYRFU] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity).

About this Structure

4hhe is a 1 chain structure with sequence from Pyrococcus furiosus. This structure supersedes the now removed PDB entry 2qs0. Full crystallographic information is available from OCA.

Reference

  • Soriano EV, Zhang Y, Colabroy KL, Sanders JM, Settembre EC, Dorrestein PC, Begley TP, Ealick SE. Active-site models for complexes of quinolinate synthase with substrates and intermediates. Acta Crystallogr D Biol Crystallogr. 2013 Sep 1;69(Pt 9):1685-96. doi:, 10.1107/S090744491301247X. Epub 2013 Aug 15. PMID:23999292 doi:10.1107/S090744491301247X

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