1fye
From Proteopedia
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|PDB= 1fye |SIZE=350|CAPTION= <scene name='initialview01'>1fye</scene>, resolution 1.20Å | |PDB= 1fye |SIZE=350|CAPTION= <scene name='initialview01'>1fye</scene>, resolution 1.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fy2|1FY2]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fye OCA], [http://www.ebi.ac.uk/pdbsum/1fye PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fye RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Miller, C G.]] | [[Category: Miller, C G.]] | ||
[[Category: Wang, A H.J.]] | [[Category: Wang, A H.J.]] | ||
| - | [[Category: CD]] | ||
[[Category: catalytic triad]] | [[Category: catalytic triad]] | ||
[[Category: peptidase]] | [[Category: peptidase]] | ||
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[[Category: strand-helix motif]] | [[Category: strand-helix motif]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:32:39 2008'' |
Revision as of 17:32, 30 March 2008
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| , resolution 1.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1FY2
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ASPARTYL DIPEPTIDASE (ANISOTROPIC B-FACTOR REFINEMENT)
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
1FYE 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
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