1ezm
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| , resolution 1.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Pseudolysin, with EC number 3.4.24.26 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURE OF THE ELASTASE OF PSEUDOMONAS AERUGINOSA AT 1.5 ANGSTROMS RESOLUTION
OverviewOverview
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.
About this StructureAbout this Structure
1EZM is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
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
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