1EZM

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

Summary for 1EZM

Entry DOI	10.2210/pdb1ezm/pdb
Descriptor	PSEUDOMONAS ELASTASE, ZINC ION, CALCIUM ION, ... (4 entities in total)
Functional Keywords	hydrolase
Biological source	Pseudomonas aeruginosa
Cellular location	Secreted: P14756
Total number of polymer chains	1
Total formula weight	33281.02
Authors	Thayer, M.M.,Flaherty, K.M.,Mckay, D.B. (deposition date: 1992-01-13, release date: 1993-10-31, Last modification date: 2024-10-23)
Primary citation	Thayer, M.M.,Flaherty, K.M.,McKay, D.B. Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution. J.Biol.Chem., 266:2864-2871, 1991 Cited by PubMed Abstract: 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. PubMed: 1899664 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.5 Å)

Structure validation