3C7U

Structural Insight into the Kinetics and Cp of interactions between TEM-1-Lactamase and BLIP

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
AMR Gene: CARD Annotation
AMR Gene Family: CARD Annotation
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3c7ua_	Multi-domain proteins (alpha and beta)	beta-lactamase/transpeptidase-like	beta-lactamase/transpeptidase-like	beta-Lactamase/D-ala carboxypeptidase	beta-Lactamase, class A	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d3c7uc_	Multi-domain proteins (alpha and beta)	beta-lactamase/transpeptidase-like	beta-lactamase/transpeptidase-like	beta-Lactamase/D-ala carboxypeptidase	beta-Lactamase, class A	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d3c7ub_	Alpha and beta proteins (a+b)	BLIP-like	beta-lactamase-inhibitor protein, BLIP	beta-lactamase-inhibitor protein, BLIP	automated matches	(Streptomyces clavuligerus ) [TaxId: 1901 ],	SCOPe (2.08)
D	d3c7ud_	Alpha and beta proteins (a+b)	BLIP-like	beta-lactamase-inhibitor protein, BLIP	beta-lactamase-inhibitor protein, BLIP	automated matches	(Streptomyces clavuligerus ) [TaxId: 1901 ],	SCOPe (2.08)

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	8041576	3001604	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	beta-lactamase/transpeptidase-like	8041576	3001604	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	BLIP repeat-like	8041615	3000321	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	BLIP repeat-like	8092081	3000321	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	BLIP repeat-like	8092081	3000321	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	BLIP repeat-like	8041615	3000321	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Peptidase_S11_1st_1	e3c7uA3	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	e3c7uA4	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)
C	Peptidase_S11_1st_1	e3c7uC3	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)
C	Beta-lactamase2	e3c7uC4	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)
B	BLIP	e3c7uB1	A: a+b two layers	X: BLIP-like	H: beta-lactamase-inhibitor protein, BLIP (From Topology)	T: beta-lactamase-inhibitor protein, BLIP	F: BLIP	ECOD (1.6)
D	BLIP	e3c7uD1	A: a+b two layers	X: BLIP-like	H: beta-lactamase-inhibitor protein, BLIP (From Topology)	T: beta-lactamase-inhibitor protein, BLIP	F: BLIP	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)
C	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)
B	3.30.1450.10	Alpha Beta	2-Layer Sandwich	Beta-lactamase Inhibitory Protein	Chain:B, domain 1	CATH (4.3.0)
D	3.30.1450.10	Alpha Beta	2-Layer Sandwich	Beta-lactamase Inhibitory Protein	Chain:B, domain 1	CATH (4.3.0)

AMR Gene: CARD Annotation CARD Database Homepage

Chains	Accession	Short Name	Description	Provenance Source (Version)
A, C	ARO:3000979	TEM-116	TEM-116 is a broad-spectrum beta-lactamase found in many species of bacteria.	CARD (3.2.9)

AMR Gene Family: CARD Annotation CARD Database Homepage

Chains	Accession	Gene Family	Drug Class	Resistance Machanism	Provenance Source (Version)
A, C	ARO:3000014	TEM beta-lactamase	monobactam, cephalosporin, penam, penem	antibiotic inactivation	CARD (3.2.9)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C	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, C	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
B, D	PF07467	Beta-lactamase inhibitor (BLIP) (BLIP)	Beta-lactamase inhibitor (BLIP)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	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	organonitrogen compound catabolic process beta-lactam antibiotic metabolic process catabolic process organonitrogen compound metabolic process lactam catabolic process organic cyclic compound catabolic process antibiotic catabolic process lactam metabolic process organic cyclic compound metabolic process amine metabolic process antibiotic metabolic process beta-lactam antibiotic catabolic process organic substance metabolic process metabolic process organonitrogen compound catabolic process beta-lactam antibiotic metabolic process catabolic process organonitrogen compound metabolic process lactam catabolic process organic cyclic compound catabolic process antibiotic catabolic process lactam metabolic process organic cyclic compound metabolic process amine metabolic process antibiotic metabolic process beta-lactam antibiotic catabolic process organic substance metabolic process metabolic process small molecule metabolic process amide metabolic process organic substance catabolic process response to stimulus response to chemical response to antibiotic	-
B, D	Beta-lactamase inhibitory protein	-	regulation of molecular function regulation of catalytic activity regulation of hydrolase activity biological regulation regulation of beta-lactamase activity	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C	IPR045155	Beta-lactamase class A, catalytic domain	Domain
A, C	IPR012338	Beta-lactamase/transpeptidase-like	Homologous Superfamily
A, C	IPR000871	Beta-lactamase, class-A	Family
A, C	IPR023650	Beta-lactamase, class-A active site	Active Site
B, D	IPR037873	BamE-like	Homologous Superfamily
B, D	IPR024221	Beta-lactamase-inhibitor protein BLIP domain superfamily	Homologous Superfamily
B, D	IPR009099	Beta-lactamase-inhibitor protein BLIP	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.