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2iv1

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'''Unreleased structure'''
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{{Seed}}
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[[Image:2iv1.jpg|left|200px]]
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The entry 2iv1 is ON HOLD until sometime in the future
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{{STRUCTURE_2iv1| PDB=2iv1 | SCENE= }}
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Authors: GUILLOTON, M., WALSH, M.A., JOACHIMIAK, A., M, P., ANDERSON,
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===SITE DIRECTED MUTAGENESIS OF KEY RESIDUES INVOLVED IN THE CATALYTIC MECHANISM OF CYANASE===
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Description: SITE DIRECTED MUTAGENESIS OF KEY RESIDUES INVOLVED IN THE CATALYTIC MECHANISM OF CYANASE
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 08:30:58 2008''
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(as it appears on PubMed at http://www.pubmed.gov), where 10801492 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10801492}}
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==About this Structure==
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2IV1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IV1 OCA].
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==Reference==
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Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site., Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, Joachimiak A, Structure. 2000 May 15;8(5):505-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10801492 10801492]
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[[Category: Cyanase]]
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Anderson, P M.]]
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[[Category: Guilloton, M.]]
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[[Category: Joachimiak, A.]]
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[[Category: Walsh, M A.]]
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[[Category: Cyanate degradation]]
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[[Category: Lyase]]
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[[Category: Mcsg]]
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[[Category: Midwest center for structural genomic]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 29 10:42:10 2008''

Revision as of 08:42, 29 October 2008

Template:STRUCTURE 2iv1

SITE DIRECTED MUTAGENESIS OF KEY RESIDUES INVOLVED IN THE CATALYTIC MECHANISM OF CYANASE

Template:ABSTRACT PUBMED 10801492

About this Structure

2IV1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site., Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, Joachimiak A, Structure. 2000 May 15;8(5):505-14. PMID:10801492

Page seeded by OCA on Wed Oct 29 10:42:10 2008

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