Annotations: 4ZI6

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Peptidase_M17	e4zi6A1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M17	ECOD (1.6)
A	Peptidase_M17_N	e4zi6A2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: Peptidase_M17_N	ECOD (1.6)
B	Peptidase_M17	e4zi6B1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M17	ECOD (1.6)
B	Peptidase_M17_N	e4zi6B2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: Peptidase_M17_N	ECOD (1.6)
C	Peptidase_M17	e4zi6C1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M17	ECOD (1.6)
C	Peptidase_M17_N	e4zi6C2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: Peptidase_M17_N	ECOD (1.6)
D	Peptidase_M17	e4zi6D1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M17	ECOD (1.6)
D	Peptidase_M17_N	e4zi6D2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: Peptidase_M17_N	ECOD (1.6)
E	Peptidase_M17	e4zi6E1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M17	ECOD (1.6)
E	Peptidase_M17_N	e4zi6E2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: Peptidase_M17_N	ECOD (1.6)
F	Peptidase_M17	e4zi6F1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M17	ECOD (1.6)
F	Peptidase_M17_N	e4zi6F2	A: a/b three-layered sandwiches	X: Macro domain-like (From Topology)	H: Macro domain-like (From Topology)	T: Macro domain-like	F: Peptidase_M17_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.220.10	Alpha Beta	3-Layer(aba) Sandwich	Leucine Aminopeptidase, subunit E	domain 1	CATH (4.3.0)
A	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
B	3.40.220.10	Alpha Beta	3-Layer(aba) Sandwich	Leucine Aminopeptidase, subunit E	domain 1	CATH (4.3.0)
B	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
C	3.40.220.10	Alpha Beta	3-Layer(aba) Sandwich	Leucine Aminopeptidase, subunit E	domain 1	CATH (4.3.0)
C	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
D	3.40.220.10	Alpha Beta	3-Layer(aba) Sandwich	Leucine Aminopeptidase, subunit E	domain 1	CATH (4.3.0)
D	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
E	3.40.220.10	Alpha Beta	3-Layer(aba) Sandwich	Leucine Aminopeptidase, subunit E	domain 1	CATH (4.3.0)
E	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
F	3.40.220.10	Alpha Beta	3-Layer(aba) Sandwich	Leucine Aminopeptidase, subunit E	domain 1	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	PF02789	Cytosol aminopeptidase family, N-terminal domain (Peptidase_M17_N)	Cytosol aminopeptidase family, N-terminal domain	-	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	Cytosol aminopeptidase	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	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	IPR008283	Peptidase M17, leucyl aminopeptidase, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR043472	Macro domain-like	Homologous Superfamily
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	IPR023042	Peptidase M17, leucine aminopeptidase	Family

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.