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1fy2

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{{Seed}}
 
[[Image:1fy2.png|left|200px]]
[[Image:1fy2.png|left|200px]]
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{{STRUCTURE_1fy2| PDB=1fy2 | SCENE= }}
{{STRUCTURE_1fy2| PDB=1fy2 | SCENE= }}
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===ASPARTYL DIPEPTIDASE===
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===Aspartyl Dipeptidase===
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==About this Structure==
==About this Structure==
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1FY2 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY2 OCA].
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[[1fy2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY2 OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:11106384</ref><references group="xtra"/>
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<ref group="xtra">PMID:011106384</ref><references group="xtra"/>
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[[Category: Salmonella typhimurium]]
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[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
[[Category: Hakansson, K.]]
[[Category: Hakansson, K.]]
[[Category: Miller, C G.]]
[[Category: Miller, C G.]]
[[Category: Wang, A H.J.]]
[[Category: Wang, A H.J.]]
[[Category: Catalytic triad]]
[[Category: Catalytic triad]]
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[[Category: Hydrolase]]
[[Category: Peptidase]]
[[Category: Peptidase]]
[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Strand-helix motif]]
[[Category: Strand-helix motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:24:51 2009''
 

Revision as of 11:36, 16 November 2011

Template:STRUCTURE 1fy2

Aspartyl Dipeptidase

Template:ABSTRACT PUBMED 11106384

About this Structure

1fy2 is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar typhimurium. Full crystallographic information is available from OCA.

Reference

  • Hakansson K, Wang AH, Miller CG. The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad. Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14097-102. PMID:11106384 doi:10.1073/pnas.260376797

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