3N8S

Crystal Structure of BlaC-E166A covalently bound with Cefamandole

Summary for 3N8S

Entry DOI	10.2210/pdb3n8s/pdb
Descriptor	Beta-lactamase, PHOSPHATE ION, (2R)-2-[(1R)-1-{[(2R)-2-hydroxy-2-phenylacetyl]amino}-2-oxoethyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid, ... (4 entities in total)
Functional Keywords	penicillin binding protein, beta-lactam covalent adduct, hydrolase-antibiotic complex, hydrolase/antibiotic
Biological source	Mycobacterium tuberculosis
Total number of polymer chains	1
Total formula weight	28869.15
Authors	Tremblay, L.W.,Blanchard, J.S. (deposition date: 2010-05-28, release date: 2010-11-24, Last modification date: 2017-11-08)
Primary citation	Tremblay, L.W.,Xu, H.,Blanchard, J.S. Structures of the Michaelis Complex (1.2 A) and the Covalent Acyl Intermediate (2.0 A) of Cefamandole Bound in the Active Sites of the Mycobacterium tuberculosis beta-Lactamase K73A and E166A Mutants. Biochemistry, 49:9685-9687, 2010 Cited by PubMed: 20961112 DOI: 10.1021/bi1015088 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation