Annotations: 5NSQ

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00883	e5nsqA2	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF00883	ECOD (1.6)
A	PF18295	e5nsqA3	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: PF18295	ECOD (1.6)
B	PF00883	e5nsqB1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF00883	ECOD (1.6)
B	PF18295	e5nsqB2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: PF18295	ECOD (1.6)
C	PF00883	e5nsqC1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF00883	ECOD (1.6)
C	PF18295	e5nsqC2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: PF18295	ECOD (1.6)
D	PF00883	e5nsqD2	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF00883	ECOD (1.6)
D	PF18295	e5nsqD3	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: PF18295	ECOD (1.6)
E	PF00883	e5nsqE2	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF00883	ECOD (1.6)
E	PF18295	e5nsqE3	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: PF18295	ECOD (1.6)
F	PF00883	e5nsqF1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF00883	ECOD (1.6)
F	PF18295	e5nsqF2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: PF18295	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.10590	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Zn-dependent exopeptidases	CATH (4.3.0)
A	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
B	3.40.50.10590	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Zn-dependent exopeptidases	CATH (4.3.0)
B	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
C	3.40.50.10590	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Zn-dependent exopeptidases	CATH (4.3.0)
C	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
D	3.40.50.10590	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Zn-dependent exopeptidases	CATH (4.3.0)
D	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
E	3.40.50.10590	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Zn-dependent exopeptidases	CATH (4.3.0)
E	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
F	3.40.50.10590	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Zn-dependent exopeptidases	CATH (4.3.0)
F	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF18295	M17 aminopeptidase N-terminal domain 2 (Pdase_M17_N2)	M17 aminopeptidase N-terminal domain 2	This domain is found in the N-terminal region of M17 aminopeptidase (Pfam:PF00883) present in Homo sapiens and Mus musculus. M17 aminopeptidases are Zn-dependent exopeptidases that catalyse the removal of unsubstituted amino acid residues from the N- ...	This domain is found in the N-terminal region of M17 aminopeptidase (Pfam:PF00883) present in Homo sapiens and Mus musculus. M17 aminopeptidases are Zn-dependent exopeptidases that catalyse the removal of unsubstituted amino acid residues from the N-terminus of peptides [1].	Domain
A, B, C, D, E A, B, C, D, E, F	PF00883	Cytosol aminopeptidase family, catalytic domain (Peptidase_M17)	Cytosol aminopeptidase family, catalytic domain	The two associated zinc ions and the active site are entirely enclosed within the C-terminal catalytic domain in leucine aminopeptidase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Aminopeptidase, putative	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein hydrolase activity metallopeptidase activity aminopeptidase activity metalloaminopeptidase activity exopeptidase activity cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein hydrolase activity metallopeptidase activity aminopeptidase activity metalloaminopeptidase activity exopeptidase activity catalytic activity metalloexopeptidase activity	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR000819	Peptidase M17, leucyl aminopeptidase, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR011356	Peptidase M17, leucine aminopeptidase/peptidase B	Family
A, B, C, D, E A, B, C, D, E, F	IPR041417	Probable aminopeptidase NPEPL1, N-terminal	Domain

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 R01GM133198.