1OME
CRYSTAL STRUCTURE OF THE OMEGA LOOP DELETION MUTANT (RESIDUES 163-178 DELETED) OF BETA-LACTAMASE FROM STAPHYLOCOCCUS AUREUS PC1
Summary for 1OME
Entry DOI | 10.2210/pdb1ome/pdb |
Descriptor | BETA-LACTAMASE, CHLORIDE ION (3 entities in total) |
Functional Keywords | hydrolase, beta-lactamase, beta-lactam antibiotic resistance |
Biological source | Staphylococcus aureus |
Total number of polymer chains | 2 |
Total formula weight | 57984.26 |
Authors | Banerjee, S.,Pieper, U.,Herzberg, O. (deposition date: 1998-02-09, release date: 1998-05-27, Last modification date: 2023-08-09) |
Primary citation | Banerjee, S.,Pieper, U.,Kapadia, G.,Pannell, L.K.,Herzberg, O. Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase. Biochemistry, 37:3286-3296, 1998 Cited by PubMed: 9521648DOI: 10.1021/bi972127f PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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