1v2g
From Proteopedia
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[[Image:1v2g.png|left|200px]] | [[Image:1v2g.png|left|200px]] | ||
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{{STRUCTURE_1v2g| PDB=1v2g | SCENE= }} | {{STRUCTURE_1v2g| PDB=1v2g | SCENE= }} | ||
===The L109P mutant of E. coli Thioesterase I/Protease I/Lysophospholipase L1 (TAP) in complexed with octanoic acid=== | ===The L109P mutant of E. coli Thioesterase I/Protease I/Lysophospholipase L1 (TAP) in complexed with octanoic acid=== | ||
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| - | (as it appears on PubMed at http://www.pubmed.gov), where 15697222 is the PubMed ID number. | ||
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{{ABSTRACT_PUBMED_15697222}} | {{ABSTRACT_PUBMED_15697222}} | ||
==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]. | + | [[1v2g]] is a 1 chain structure of [[Thioesterase]] 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]. |
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| + | ==See Also== | ||
| + | *[[Thioesterase|Thioesterase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015697222</ref><ref group="xtra">PMID:012842470</ref><references group="xtra"/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Liaw, Y C.]] | [[Category: Liaw, Y C.]] | ||
[[Category: Lin, S C.]] | [[Category: Lin, S C.]] | ||
[[Category: Lo, Y C.]] | [[Category: Lo, Y C.]] | ||
| + | [[Category: Hydrolase]] | ||
[[Category: Sgnh-hydrolase fold]] | [[Category: Sgnh-hydrolase fold]] | ||
Revision as of 21:26, 25 July 2012
Contents |
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 of Thioesterase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
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
