Annotations: 4BIN

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	AMIN domain-like	8046923	4005368	SCOP2 (2022-06-29)
A	SCOP2 Family	N-acetylmuramoyl-L-alanine amidase-like	8092183	4001130	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	AMIN domain-like	8092182	3002568	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Zn-dependent exopeptidases	8092184	3000662	SCOP2 (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	PF11741	e4binA2	A: beta sandwiches	X: HSP20-like	H: B2 domain of PilQ (From Topology)	T: B2 domain of PilQ	F: PF11741	ECOD (1.6)
A	PF01520	e4binA1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF01520	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.3500	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
A	3.40.630.40	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn-dependent exopeptidases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF11741	AMIN domain (AMIN)	AMIN domain	-	Family
A	PF01520	N-acetylmuramoyl-L-alanine amidase (Amidase_3)	N-acetylmuramoyl-L-alanine amidase	This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC	peptidoglycan muralytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity N-acetylmuramoyl-L-alanine amidase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds	organonitrogen compound catabolic process carbohydrate derivative catabolic process organonitrogen compound metabolic process catabolic process peptidoglycan catabolic process glycosaminoglycan metabolic process carbohydrate derivative metabolic process aminoglycan catabolic process macromolecule catabolic process glycosaminoglycan catabolic process organic substance metabolic process aminoglycan metabolic process peptidoglycan metabolic process metabolic process organonitrogen compound catabolic process carbohydrate derivative catabolic process organonitrogen compound metabolic process catabolic process peptidoglycan catabolic process glycosaminoglycan metabolic process carbohydrate derivative metabolic process aminoglycan catabolic process macromolecule catabolic process glycosaminoglycan catabolic process organic substance metabolic process aminoglycan metabolic process peptidoglycan metabolic process metabolic process macromolecule metabolic process organic substance catabolic process cellular component organization cell wall organization or biogenesis cell wall organization cellular process cellular component organization or biogenesis external encapsulating structure organization reproductive process in single-celled organism reproductive process cytokinesis cell division cell cycle FtsZ-dependent cytokinesis cell cycle process asexual reproduction	periplasmic space cellular anatomical entity outer membrane-bounded periplasmic space cell envelope

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A	IPR021731	AMIN domain	Domain
A	IPR002508	N-acetylmuramoyl-L-alanine amidase, catalytic domain	Domain

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.