1v2g
From Proteopedia
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[[Image:1v2g.png|left|200px]] | [[Image:1v2g.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1v2g]] is a 1 chain structure with 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=1V2G OCA]. | |
==Reference== | ==Reference== | ||
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[[Category: Lo, Y C.]] | [[Category: Lo, Y C.]] | ||
[[Category: Sgnh-hydrolase fold]] | [[Category: Sgnh-hydrolase fold]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 18:58:36 2009'' | ||
Revision as of 20:59, 14 March 2011
The L109P mutant of E. coli Thioesterase I/Protease I/Lysophospholipase L1 (TAP) in complexed with octanoic acid
Template:ABSTRACT PUBMED 15697222
About this Structure
1v2g is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Lo YC, Lin SC, Shaw JF, Liaw YC. Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement. Biochemistry. 2005 Feb 15;44(6):1971-9. PMID:15697222 doi:10.1021/bi048109x
- Lo YC, Lin SC, Shaw JF, Liaw YC. Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network. J Mol Biol. 2003 Jul 11;330(3):539-51. PMID:12842470
