1GHP
STRUCTURES OF THE ACYL-ENZYME COMPLEX OF THE STAPHYLOCOCCUS AUREUS BETA-LACTAMASE MUTANT GLU166ASP:ASN170GLN WITH DEGRADED BENZYLPENICILLIN
Summary for 1GHP
Entry DOI | 10.2210/pdb1ghp/pdb |
Descriptor | BETA-LACTAMASE, SULFATE ION, OPEN FORM - PENICILLIN G, ... (4 entities in total) |
Functional Keywords | hydrolase, antibiotic resistance, beta-lactam hydrolysis, benzylpenicillin, cephaloridine |
Biological source | Staphylococcus aureus |
Total number of polymer chains | 1 |
Total formula weight | 29695.07 |
Authors | Chen, C.C.H.,Herzberg, O. (deposition date: 2000-12-21, release date: 2001-04-04, Last modification date: 2023-08-09) |
Primary citation | Chen, C.C.,Herzberg, O. Structures of the acyl-enzyme complexes of the Staphylococcus aureus beta-lactamase mutant Glu166Asp:Asn170Gln with benzylpenicillin and cephaloridine. Biochemistry, 40:2351-2358, 2001 Cited by PubMed: 11327855DOI: 10.1021/bi002277h PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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