1pio is a 2 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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 beta-lactamase from Staphylococcus aureus PC1 has been cloned into an Escherichia coli vector for site-directed mutagenesis and high-level protein expression. A mutant enzyme has been produced in which Ala238 is replaced by a serine, and Ile239 is deleted (A238S:I239del). The engineered enzyme hydrolyses third-generation cephalosporins substantially more rapidly than the parental enzyme does, while hydrolysis of benzylpenicillin is slower with the mutant than with the wild-type and native enzymes. The mutant beta-lactamase has been crystallized and the structure determined and refined at 2.8 A resolution. The disposition of the beta-strand which forms the side of the active site is altered in comparison with the native S. aureus beta-lactamase structure, widening the active site cleft and providing space to accommodate the bulky side-chains of the third-generation cephalosporins.
An engineered Staphylococcus aureus PC1 beta-lactamase that hydrolyses third-generation cephalosporins.,Zawadzke LE, Smith TJ, Herzberg O Protein Eng. 1995 Dec;8(12):1275-85. PMID:8869640[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Zawadzke LE, Smith TJ, Herzberg O. An engineered Staphylococcus aureus PC1 beta-lactamase that hydrolyses third-generation cephalosporins. Protein Eng. 1995 Dec;8(12):1275-85. PMID:8869640
