Annotations: 1ZNB

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1znba_	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	Zn metallo-beta-lactamase	Zn metallo-beta-lactamase	(Bacteroides fragilis ) [TaxId: 817 ],	SCOPe (2.08)
B	d1znbb_	Alpha and beta proteins (a+b)	Metallo-hydrolase/oxidoreductase	Metallo-hydrolase/oxidoreductase	Zn metallo-beta-lactamase	Zn metallo-beta-lactamase	(Bacteroides fragilis ) [TaxId: 817 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Metallo-hydrolase/oxidoreductase	8036850	3001057	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Metallo-hydrolase/oxidoreductase	8036850	3001057	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	Lactamase_B	e1znbA1	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: Lactamase_B	ECOD (1.6)
B	Lactamase_B	e1znbB1	A: a+b four layers	X: Metallo-hydrolase/oxidoreductase (From Topology)	H: Metallo-hydrolase/oxidoreductase (From Topology)	T: Metallo-hydrolase/oxidoreductase	F: Lactamase_B	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.60.15.10	Alpha Beta	4-Layer Sandwich	Metallo-beta-lactamase	Chain A	CATH (4.3.0)
B	3.60.15.10	Alpha Beta	4-Layer Sandwich	Metallo-beta-lactamase	Chain A	CATH (4.3.0)

AMR Gene: CARD Annotation CARD Database Homepage

Chains	Accession	Short Name	Description	Provenance Source (Version)
A, B	ARO:3006912	CfiA2	CfiA2 is a CfiA beta-lactamase.	CARD (3.2.9)

AMR Gene Family: CARD Annotation CARD Database Homepage

Chains	Accession	Gene Family	Drug Class	Resistance Machanism	Provenance Source (Version)
A, B	ARO:3004200	CfiA beta-lactamase	carbapenem	antibiotic inactivation	CARD (3.2.9)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	METALLO-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 cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	antibiotic metabolic process catabolic process metabolic process antibiotic catabolic process response to stimulus response to chemical response to antibiotic	periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001018	Beta-lactamase, class-B, conserved site	Conserved Site
A, B	IPR036866	Ribonuclease Z/Hydroxyacylglutathione hydrolase-like	Homologous Superfamily
A, B	IPR001279	Metallo-beta-lactamase	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	beta-lactamase (Class B1) M-CSA #15	Beta-lactamase is a key enzyme in antibiotic resistance, catalysing the cleavage of the essential beta-lactam ring structure in penicillin and cephalosporinase type antibiotics. Substrate specificity varies considerably within the beta-lactamases, with some enzymes preferring penicillins and some cephalosporins. Alongside the class B beta-lactamases, described here, there also exist three other classes of beta-lactam cleaving enzymes (A,C and D). These groups of enzymes use a serine nucleophilic mechanism, while class B uses a mono/dimetallic zinc mechanism. This entry describes the dimetallic mechanism. There is considerable variety in substrate specificity between the classes, although class C enzymes tend to have a high cephalosporinase activity	Defined by 8 residues: HIS:A-82 [auth A-99]HIS:A-84 [auth A-101]ASP:A-86 [auth A-103]HIS:A-145 [auth A-162]CYS:A-164 [auth A-181]LYS:A-167 [auth A-184]ASN:A-176 [auth A-193]HIS:A-206 [auth A-223] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.5.2.6 (PDB Primary Data) Search M-CSA Motif + EC 3.5.2.6

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