8GCX

XFEL structure of Mycobacterium tuberculosis beta lactamase microcrystals mixed with sulbactam for 700 ms

External Resource: Annotation

Domain Annotation: SCOP2 Classification
AMR Gene: CARD Annotation
AMR Gene Family: CARD Annotation
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	beta-lactamase/transpeptidase-like	8069823	3001604	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	beta-lactamase/transpeptidase-like	8069823	3001604	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	beta-lactamase/transpeptidase-like	8069823	3001604	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	beta-lactamase/transpeptidase-like	8069823	3001604	SCOP2B (2022-06-29)

AMR Gene: CARD Annotation CARD Database Homepage

Chains	Accession	Short Name	Description	Provenance Source (Version)
A, B, C, D	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)

AMR Gene Family: CARD Annotation CARD Database Homepage

Chains	Accession	Gene Family	Drug Class	Resistance Machanism	Provenance Source (Version)
A, B, C, D	ARO:3007181	class A Mycobacterium tuberculosis bla beta-lactamase	cephalosporin, cephamycin, penam, penem	antibiotic inactivation	CARD (3.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF13354	Beta-lactamase enzyme family (Beta-lactamase2)	Beta-lactamase enzyme family	This is the catalytic domain of class A beta-lactamases [1]. It is closely related to Beta-lactamase, Pfam:PF00144, the serine beta-lactamase-like superfamily, which contains the distantly related Pfam:PF00905 and PF00768 D-alanyl-D-alanine carboxype ...	This is the catalytic domain of class A beta-lactamases [1]. It is closely related to Beta-lactamase, Pfam:PF00144, the serine beta-lactamase-like superfamily, which contains the distantly related Pfam:PF00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	Domain
A, B, C, D	PF00144	Beta-lactamase (Beta-lactamase)	Beta-lactamase	This family appears to be distantly related to Pfam:PF00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Beta-lactamase	beta-lactamase activity hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds	beta-lactam antibiotic metabolic process catabolic process lactam catabolic process antibiotic catabolic process lactam metabolic process amine metabolic process antibiotic metabolic process beta-lactam antibiotic catabolic process metabolic process cellular process small molecule metabolic process amide metabolic process response to stimulus response to chemical beta-lactam antibiotic metabolic process catabolic process lactam catabolic process antibiotic catabolic process lactam metabolic process amine metabolic process antibiotic metabolic process beta-lactam antibiotic catabolic process metabolic process cellular process small molecule metabolic process amide metabolic process response to stimulus response to chemical response to antibiotic	cell periphery cellular anatomical structure plasma membrane membrane periplasmic space extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR045155	Beta-lactamase class A, catalytic domain	Domain
A, B, C, D	IPR012338	Beta-lactamase/transpeptidase-like	Homologous Superfamily
A, B, C, D	IPR000871	Beta-lactamase, class-A	Family
A, B, C, D	IPR023650	Beta-lactamase, class-A active site	Active Site

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.