1amu

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[[Image:1amu.png|left|200px]]
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{{STRUCTURE_1amu| PDB=1amu | SCENE= }}
{{STRUCTURE_1amu| PDB=1amu | SCENE= }}
===PHENYLALANINE ACTIVATING DOMAIN OF GRAMICIDIN SYNTHETASE 1 IN A COMPLEX WITH AMP AND PHENYLALANINE===
===PHENYLALANINE ACTIVATING DOMAIN OF GRAMICIDIN SYNTHETASE 1 IN A COMPLEX WITH AMP AND PHENYLALANINE===
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{{ABSTRACT_PUBMED_9250661}}
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==About this Structure==
==About this Structure==
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1AMU is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMU OCA].
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[[1amu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AMU OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:9250661</ref><references group="xtra"/>
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<ref group="xtra">PMID:009250661</ref><ref group="xtra">PMID:010933494</ref><references group="xtra"/>
[[Category: Brevibacillus brevis]]
[[Category: Brevibacillus brevis]]
[[Category: Brick, P.]]
[[Category: Brick, P.]]
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[[Category: Grsa]]
[[Category: Grsa]]
[[Category: Peptide synthetase]]
[[Category: Peptide synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:56:55 2009''
 

Revision as of 11:48, 21 October 2012

Template:STRUCTURE 1amu

PHENYLALANINE ACTIVATING DOMAIN OF GRAMICIDIN SYNTHETASE 1 IN A COMPLEX WITH AMP AND PHENYLALANINE

Template:ABSTRACT PUBMED 9250661

About this Structure

1amu is a 2 chain structure with sequence from Brevibacillus brevis. Full crystallographic information is available from OCA.

Reference

  • Conti E, Stachelhaus T, Marahiel MA, Brick P. Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S. EMBO J. 1997 Jul 16;16(14):4174-83. PMID:9250661
  • Jung JW, An JH, Na KB, Kim YS, Lee W. The active site and substrates binding mode of malonyl-CoA synthetase determined by transferred nuclear Overhauser effect spectroscopy, site-directed mutagenesis, and comparative modeling studies. Protein Sci. 2000 Jul;9(7):1294-303. PMID:10933494 doi:10.1110/ps.9.7.1294

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