This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1fy2
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1fy2.jpg|left|200px]] | + | [[Image:1fy2.jpg|left|200px]] |
| - | + | ||
| - | '''ASPARTYL DIPEPTIDASE''' | + | {{Structure |
| + | |PDB= 1fy2 |SIZE=350|CAPTION= <scene name='initialview01'>1fy2</scene>, resolution 1.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ASPARTYL DIPEPTIDASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1FY2 is a [ | + | 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== | ||
| - | 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:// | + | 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]] | ||
| Line 22: | Line 31: | ||
[[Category: strand-helix motif]] | [[Category: strand-helix motif]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''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
| |||||||
| , 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
