Annotations: 1LML

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1lmla_	Alpha and beta proteins (a+b)	Zincin-like	Metalloproteases ('zincins'), catalytic domain	Leishmanolysin	Leishmanolysin	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Leishmanolysin	8023080	4001619	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Metalloproteases (zincins) catalytic domain	8035460	3001975	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	Peptidase_M8	e1lmlA1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: Peptidase_M8	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.170.20	Alpha Beta	Roll	Elastase	domain 1	CATH (4.3.0)
A	3.90.132.10	Alpha Beta	Alpha-Beta Complex	Leishmanolysin	domain 2	CATH (4.3.0)
A	2.10.55.10	Mainly Beta	Ribbon	Leishmanolysin	domain 3	CATH (4.3.0)
A	2.30.34.10	Mainly Beta	Roll	Leishmanolysin	domain 4	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01457	Leishmanolysin (Peptidase_M8)	Leishmanolysin	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	LEISHMANOLYSIN	peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding metalloendopeptidase activity endopeptidase activity	symbiont-mediated perturbation of host defense response response to host defenses biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to defenses of other organism response to external stimulus response to biotic stimulus biological process involved in interaction with host biological process involved in symbiotic interaction modulation by symbiont of host process response to host response to external biotic stimulus symbiont-mediated perturbation of host inflammatory response symbiont-mediated perturbation of host defense response response to host defenses biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to defenses of other organism response to external stimulus response to biotic stimulus biological process involved in interaction with host biological process involved in symbiotic interaction modulation by symbiont of host process response to host response to external biotic stimulus symbiont-mediated perturbation of host inflammatory response modulation of process of another organism organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process symbiont-mediated perturbation of host cellular process cellular process symbiont-mediated activation of host signal transduction pathway symbiont-mediated perturbation of host signal transduction pathway cell adhesion	membrane cellular anatomical entity side of membrane cell periphery plasma membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001577	Peptidase M8, leishmanolysin	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	leishmanolysin M-CSA #668	Leishmania is a protozoan parasite transmitted from sandfly vector to human and other mammalian hosts causing chronic infections. It exists as extracellular promastigotes within sandflies and intracellular amastigotes within macrophage cells of mammals. Leishmanolysin is the major protein component of the Leishmania promastigote surface. It is characterised as a zinc metalloproteinase containing a glycosyl phosphatidyl inositol membrane anchor. It is an endopeptidase cleaving a variety of substrate. Its role in the life cycle Leishmania remains to be established.	Defined by 4 residues: HIS:A-165 [auth A-264]GLU:A-166 [auth A-265]HIS:A-169 [auth A-268]HIS:A-235 [auth A-334] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.4.24.36 (PDB Primary Data) Search M-CSA Motif + EC 3.4.24.36

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.