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2x30

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[[Image:2x30.png|left|200px]]
[[Image:2x30.png|left|200px]]
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{{STRUCTURE_2x30| PDB=2x30 | SCENE= }}
{{STRUCTURE_2x30| PDB=2x30 | SCENE= }}
===CRYSTAL STRUCTURE OF THE R139N MUTANT OF A BIFUNCTIONAL ENZYME PRIA===
===CRYSTAL STRUCTURE OF THE R139N MUTANT OF A BIFUNCTIONAL ENZYME PRIA===
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{{ABSTRACT_PUBMED_20066665}}
{{ABSTRACT_PUBMED_20066665}}
==About this Structure==
==About this Structure==
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2X30 is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X30 OCA].
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[[2x30]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X30 OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:20066665</ref><references group="xtra"/>
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<ref group="xtra">PMID:020066665</ref><references group="xtra"/>
[[Category: Streptomyces coelicolor]]
[[Category: Streptomyces coelicolor]]
[[Category: Barona-Gomez, F.]]
[[Category: Barona-Gomez, F.]]
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[[Category: Trpf]]
[[Category: Trpf]]
[[Category: Tryptophan biosynthesis]]
[[Category: Tryptophan biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 26 08:37:48 2010''
 

Revision as of 22:04, 7 January 2013

Template:STRUCTURE 2x30

CRYSTAL STRUCTURE OF THE R139N MUTANT OF A BIFUNCTIONAL ENZYME PRIA

Template:ABSTRACT PUBMED 20066665

About this Structure

2x30 is a 1 chain structure with sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA.

Reference

  • Noda-Garcia L, Camacho-Zarco AR, Verdel-Aranda K, Wright H, Soberon X, Fulop V, Barona-Gomez F. Identification and analysis of residues contained on beta --> alpha loops of the dual-substrate (betaalpha)(8) phosphoribosyl isomerase a (PriA) specific for its phosphoribosyl anthranilate isomerase activity. Protein Sci. 2010 Jan 11. PMID:20066665 doi:10.1002/pro.331

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