1fy2 | pdb_00001fy2

Aspartyl Dipeptidase

spinqualitylabelsall models 1fy2, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fy2 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD Related: 1fye Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PEPE_SALTY] Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.[HAMAP-Rule:MF_00510] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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