Annotations: 3QS1

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Acid proteases	8066353	3001059	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Acid proteases	8066353	3001059	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Acid proteases	8066353	3001059	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Acid proteases	8066353	3001059	SCOP2B (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	Asp_C	e3qs1A3	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_C	ECOD (1.6)
A	Asp_N	e3qs1A2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_N	ECOD (1.6)
B	Asp_C	e3qs1B3	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_C	ECOD (1.6)
B	Asp_N	e3qs1B2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_N	ECOD (1.6)
C	Asp_C	e3qs1C3	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_C	ECOD (1.6)
C	Asp_N	e3qs1C2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_N	ECOD (1.6)
D	Asp_C	e3qs1D3	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_C	ECOD (1.6)
D	Asp_N	e3qs1D2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)
B	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)
C	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)
D	2.40.70.10	Mainly Beta	Beta Barrel	Cathepsin D, subunit A	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00026	Eukaryotic aspartyl protease (Asp)	Eukaryotic aspartyl protease	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Plasmepsin-1	aspartic-type peptidase activity peptidase activity catalytic activity, acting on a protein hydrolase activity aspartic-type endopeptidase activity catalytic activity endopeptidase activity	biological process involved in interspecies interaction between organisms acquisition of nutrients from host biological process involved in interaction with host biological process involved in symbiotic interaction proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	cell periphery cellular anatomical structure plasma membrane membrane cytostome vacuolar membrane membrane-bounded organelle intracellular anatomical structure vacuole intracellular membrane-bounded organelle intracellular organelle bounding membrane of organelle organelle cytoplasm cell periphery cellular anatomical structure plasma membrane membrane cytostome vacuolar membrane membrane-bounded organelle intracellular anatomical structure vacuole intracellular membrane-bounded organelle intracellular organelle bounding membrane of organelle organelle cytoplasm organelle membrane phagolysosome lytic vacuole intracellular vesicle phagocytic vesicle food vacuole cytoplasmic vesicle secondary lysosome vesicle endocytic vesicle lysosome membrane-enclosed lumen vacuolar lumen intracellular organelle lumen organelle lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR001461	Aspartic peptidase A1	Family
A, B, C, D	IPR033121	Peptidase family A1 domain	Domain
A, B, C, D	IPR034164	Pepsin-like domain	Domain
A, B, C, D	IPR021109	Aspartic peptidase domain superfamily	Homologous Superfamily
A, B, C, D	IPR001969	Aspartic peptidase, active site	Active Site

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.