1FR1
REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS
Summary for 1FR1
Entry DOI | 10.2210/pdb1fr1/pdb |
Related | 1FR6 |
Descriptor | BETA-LACTAMASE (2 entities in total) |
Functional Keywords | hydrolase, antibiotic resistance, class c beta-lactamase |
Biological source | Citrobacter freundii |
Total number of polymer chains | 2 |
Total formula weight | 79510.50 |
Authors | Oefner, C.,D'Arcy, A.,Daly, J.J.,Winkler, F.K. (deposition date: 2000-09-07, release date: 2001-01-17, Last modification date: 2024-02-07) |
Primary citation | Oefner, C.,D'Arcy, A.,Daly, J.J.,Gubernator, K.,Charnas, R.L.,Heinze, I.,Hubschwerlen, C.,Winkler, F.K. Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis. Nature, 343:284-288, 1990 Cited by PubMed: 2300174DOI: 10.1038/343284a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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