1fy2

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[[Image:1fy2.jpg|left|200px]]<br /><applet load="1fy2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fy2.jpg|left|200px]]
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caption="1fy2, resolution 1.2&Aring;" />
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'''ASPARTYL DIPEPTIDASE'''<br />
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{{Structure
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|PDB= 1fy2 |SIZE=350|CAPTION= <scene name='initialview01'>1fy2</scene>, resolution 1.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''ASPARTYL DIPEPTIDASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1FY2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY2 OCA].
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1FY2 is a [[Single protein]] 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].
==Reference==
==Reference==
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The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad., Hakansson K, Wang AH, Miller CG, Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14097-102. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11106384 11106384]
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The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad., Hakansson K, Wang AH, Miller CG, Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14097-102. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11106384 11106384]
[[Category: Salmonella typhimurium]]
[[Category: Salmonella typhimurium]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: strand-helix motif]]
[[Category: strand-helix motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:15:29 2008''

Revision as of 09:15, 20 March 2008

Image:1fy2.jpg


PDB ID 1fy2

Drag the structure with the mouse to rotate
, resolution 1.2Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



ASPARTYL DIPEPTIDASE


Overview

The three-dimensional structure of Salmonella typhimurium aspartyl dipeptidase, peptidase E, was solved crystallographically and refined to 1.2-A resolution. The structure of this 25-kDa enzyme consists of two mixed beta-sheets forming a V, flanked by six alpha-helices. The active site contains a Ser-His-Glu catalytic triad and is the first example of a serine peptidase/protease with a glutamate in the catalytic triad. The active site Ser is located on a strand-helix motif reminiscent of that found in alpha/beta-hydrolases, but the polypeptide fold and the organization of the catalytic triad differ from those of the known serine proteases. This enzyme is a member of a family of serine hydrolases and appears to represent a new example of convergent evolution of peptidase activity.

About this Structure

1FY2 is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Mar 20 11:15:29 2008

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