1pgt: Difference between revisions

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==About this Structure==
==About this Structure==
1PGT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PGT OCA].  
1PGT is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PGT OCA].  


==Reference==
==Reference==
Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase., Ji X, Tordova M, O'Donnell R, Parsons JF, Hayden JB, Gilliland GL, Zimniak P, Biochemistry. 1997 Aug 12;36(32):9690-702. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9245401 9245401]
<ref group="xtra">PMID:9245401</ref><references group="xtra"/>
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Ji, X.]]
[[Category: Ji, X.]]
[[Category: Detoxification]]
[[Category: Detoxification]]
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[[Category: Transferase]]
[[Category: Transferase]]


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Revision as of 05:13, 17 February 2009

File:1pgt.png

Template:STRUCTURE 1pgt

CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONECRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE

Template:ABSTRACT PUBMED 9245401

About this StructureAbout this Structure

1PGT is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Ji X, Tordova M, O'Donnell R, Parsons JF, Hayden JB, Gilliland GL, Zimniak P. Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase. Biochemistry. 1997 Aug 12;36(32):9690-702. PMID:9245401 doi:10.1021/bi970805s

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