3IQA
Crystal Structure of BlaC covalently bound with Doripenem
Summary for 3IQA
Entry DOI | 10.2210/pdb3iqa/pdb |
Descriptor | Beta-lactamase, PHOSPHATE ION, (2S,3R,4S)-2-[(2S,3R)-3-hydroxy-1-oxobutan-2-yl]-3-methyl-4-({(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl}sulfanyl)-3,4-dihydro-2H-pyrrole-5-carboxylic acid, ... (4 entities in total) |
Functional Keywords | penicillin binding protein, beta-lactam covalent adduct, antibiotic resistance, cell membrane, hydrolase, lipoprotein, membrane, palmitate, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 1 |
Total formula weight | 28885.18 |
Authors | Tremblay, L.W.,Blanchard, J.S. (deposition date: 2009-08-19, release date: 2010-04-14, Last modification date: 2023-09-06) |
Primary citation | Tremblay, L.W.,Fan, F.,Blanchard, J.S. Biochemical and structural characterization of Mycobacterium tuberculosis beta-lactamase with the carbapenems ertapenem and doripenem. Biochemistry, 49:3766-3773, 2010 Cited by PubMed: 20353175DOI: 10.1021/bi100232q PDB entries with the same primary citation |
Experimental method |
Structure validation
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