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Structure of BlaC from Mycobacterium tuberculosis bound to the trans-enamine adduct of sulbactam. External Resource: Annotation Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) B Peptidase_S11_1st_1 e6h2kB2 A: alpha complex topology X: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology) H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology) T: alpha-helical domain in beta-lactamase/transpeptidase-like proteins F: Peptidase_S11_1st_1 ECOD (1.6) B Beta-lactamase2 e6h2kB1 A: a+b three layers X: Profilin-like H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology) T: a+b domain in beta-lactamase/transpeptidase-like proteins F: Beta-lactamase2 ECOD (1.6) A Peptidase_S11_1st_1 e6h2kA1 A: alpha complex topology X: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology) H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology) T: alpha-helical domain in beta-lactamase/transpeptidase-like proteins F: Peptidase_S11_1st_1 ECOD (1.6) A Beta-lactamase2 e6h2kA2 A: a+b three layers X: Profilin-like H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology) T: a+b domain in beta-lactamase/transpeptidase-like proteins F: Beta-lactamase2 ECOD (1.6)
Chains Accession Short Name Description Provenance Source (Version) ARO:3007182 blaC blaC is a broad-spectrum class A beta-lactamase coded in the chromosome of Mycobacterium tuberculosis. It has been shown to hydrolyze a large number of beta-lactam antibiotics and is a major obstacle in the treatment of tuberculosis with such drugs. CARD (3.3.0)
