4K5N

Phosphonic Arginine Mimetics as Inhibitors of the M1 Aminopeptidases from Plasmodium falciparum

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	DUF3458	e4k5nA3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: DUF3458	ECOD (1.6)
A	Peptidase_M1_2	e4k5nA4	A: beta sandwiches	X: Baculovirus p35 protein-related (From Topology)	H: Baculovirus p35 protein-related (From Topology)	T: Baculovirus p35 protein-related	F: Peptidase_M1_2	ECOD (1.6)
A	DUF3458_C	e4k5nA2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: DUF3458_C	ECOD (1.6)
A	Peptidase_M1_1	e4k5nA1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Peptidase_M1_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.1730	Mainly Beta	Sandwich	Immunoglobulin-like	tricorn interacting facor f3 domain	CATH (4.3.0)
A	3.30.2010.30	Alpha Beta	2-Layer Sandwich	Zincin-like		CATH (4.3.0)
A	1.10.390.10	Mainly Alpha	Orthogonal Bundle	Neutral Protease	domain 2	CATH (4.3.0)
A	2.60.40.1840	Mainly Beta	Sandwich	Immunoglobulin-like	Aminopeptidase N, middle-beta domain	CATH (4.3.0)
A	1.25.50.10	Mainly Alpha	Alpha Horseshoe	Zincin-like fold	Peptidase M1, alanyl aminopeptidase, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF11940	Domain of unknown function (DUF3458) Ig-like fold (DUF3458)	Domain of unknown function (DUF3458) Ig-like fold	This presumed domain is functionally uncharacterised. This domain is found in bacteria, archaea and eukaryotes. The domain has an Ig-like fold. This domain is found associated with Pfam:PF01433.	Domain
A	PF17432	Domain of unknown function (DUF3458_C) ARM repeats (DUF3458_C)	Domain of unknown function (DUF3458_C) ARM repeats	-	Repeat
A	PF01433	Peptidase family M1 domain (Peptidase_M1)	Peptidase family M1 domain	Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase Swiss:P09960, this enzyme also has an aminopeptidase activ ...	Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase Swiss:P09960, this enzyme also has an aminopeptidase activity [1].	Domain
A	PF17900	Peptidase M1 N-terminal domain (Peptidase_M1_N)	Peptidase M1 N-terminal domain	This domain is found at the N-terminus of aminopeptidases from the M1 family.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	M1 family aminopeptidase	cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein hydrolase activity exopeptidase activity dipeptidase activity catalytic activity metallopeptidase activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein hydrolase activity exopeptidase activity dipeptidase activity catalytic activity metallopeptidase activity aminopeptidase activity metalloaminopeptidase activity metalloexopeptidase activity	proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	membrane cellular anatomical entity membrane-bounded organelle host cellular component host intracellular part extracellular organelle extracellular region symbiont-containing vacuole membrane host cell cytoplasm part symbiont-containing vacuole host cell cytoplasm host cell part organelle host intracellular region membrane cellular anatomical entity membrane-bounded organelle host cellular component host intracellular part extracellular organelle extracellular region symbiont-containing vacuole membrane host cell cytoplasm part symbiont-containing vacuole host cell cytoplasm host cell part organelle host intracellular region extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm phagolysosome lytic vacuole intracellular vesicle vacuole phagocytic vesicle intracellular membrane-bounded organelle food vacuole intracellular organelle cytoplasmic vesicle secondary lysosome vesicle endocytic vesicle lysosome membrane-enclosed lumen vacuolar lumen intracellular organelle lumen organelle lumen nucleus

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001930	Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase	Family
A	IPR024601	Peptidase M1, alanyl aminopeptidase, C-terminal	Domain
A	IPR012779	Peptidase M1, alanyl aminopeptidase	Family
A	IPR037144	Peptidase M1, alanyl aminopeptidase, C-terminal domain superfamily	Homologous Superfamily
A	IPR035414	Peptidase M1, alanyl aminopeptidase, Ig-like fold	Domain
A	IPR027268	Peptidase M4/M1, CTD superfamily	Homologous Superfamily
A	IPR014782	Peptidase M1, membrane alanine aminopeptidase	Domain
A	IPR045357	Aminopeptidase N-like , N-terminal domain	Domain
A	IPR042097	Aminopeptidase N-like , N-terminal domain superfamliy	Homologous Superfamily
A	IPR038438	Alanyl aminopeptidase, Ig-like domain superfamily	Homologous Superfamily

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.