2glt: Difference between revisions

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==About this Structure==
==About this Structure==
2GLT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1glt 1glt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLT OCA].  
2GLT is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1glt 1glt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GLT OCA].  


==Reference==
==Reference==
Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins., Matsuda K, Mizuguchi K, Nishioka T, Kato H, Go N, Oda J, Protein Eng. 1996 Dec;9(12):1083-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9010922 9010922]
<ref group="xtra">PMID:9010922</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutathione synthase]]
[[Category: Glutathione synthase]]
[[Category: Single protein]]
[[Category: Kato, H.]]
[[Category: Kato, H.]]
[[Category: Katsube, Y.]]
[[Category: Katsube, Y.]]
Line 35: Line 34:
[[Category: Glutathione biosynthesis ligase]]
[[Category: Glutathione biosynthesis ligase]]


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Revision as of 18:45, 16 February 2009

File:2glt.png

Template:STRUCTURE 2glt

STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 6.0.

Template:ABSTRACT PUBMED 9010922

About this Structure

2GLT is a 1 chain structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1glt. Full crystallographic information is available from OCA.

Reference

  1. Matsuda K, Mizuguchi K, Nishioka T, Kato H, Go N, Oda J. Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins. Protein Eng. 1996 Dec;9(12):1083-92. PMID:9010922

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