1ezm | pdb_00001ezm

THREE-DIMENSIONAL STRUCTURE OF THE ELASTASE OF PSEUDOMONAS AERUGINOSA AT 1.5 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1ezm, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ezm is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: CA, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ELAS_PSEAE Cleaves elastin, collagen, IgG, and several complement components. Involved in the pathogenesis of P.aeruginosa infections. 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 Pseudomonas aeruginosa elastase (PAE) is a zinc metalloprotease with 301 amino acids. We have crystallized and solved the three-dimensional structure of PAE, using data to 1.5-A resolution, and have refined the native molecular structure to R = 0.188. The overall tertiary structure of the PAE molecule is similar to that of thermolysin, with which it shares 28% amino acid sequence identity. Nearly all of the active site residues that might potentially interact with substrates are identical in the two proteins. However, the active site cleft is significantly more "open" in PAE than in thermolysin. Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution.,Thayer MM, Flaherty KM, McKay DB J Biol Chem. 1991 Feb 15;266(5):2864-71. PMID:1899664 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elastase 3D structures

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