1CEG
CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE
Summary for 1CEG
Entry DOI | 10.2210/pdb1ceg/pdb |
Descriptor | D-ALANYL-D-ALANINE CARBOXYPEPTIDASE TRANSPEPTIDASE, CEPHALOTHIN GROUP (3 entities in total) |
Functional Keywords | d-amino acid peptidase, penicillin target, hydrolase-transpeptidase |
Biological source | Streptomyces sp. |
Cellular location | Secreted: P15555 |
Total number of polymer chains | 1 |
Total formula weight | 37821.03 |
Authors | Knox, J.R.,Kuzin, A.P. (deposition date: 1995-01-12, release date: 1996-10-14, Last modification date: 2024-06-05) |
Primary citation | Kuzin, A.P.,Liu, H.,Kelly, J.A.,Knox, J.R. Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases. Biochemistry, 34:9532-9540, 1995 Cited by PubMed: 7626623DOI: 10.1021/bi00029a030 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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