Annotations: 5NFG

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Asp_C	e5nfgA2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_C	ECOD (1.6)
A	Asp_N	e5nfgA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_N	ECOD (1.6)
B	Asp_C	e5nfgB1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: Asp_C	ECOD (1.6)
B	Asp_N	e5nfgB2	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00026	Eukaryotic aspartyl protease (Asp)	Eukaryotic aspartyl protease	Aspartyl (acid) proteases include pepsins, cathepsins, and renins. Two-domain structure, probably arising from ancestral duplication. This family does not include the retroviral nor retrotransposon proteases (Pfam:PF00077), which are much smaller a ...	Aspartyl (acid) proteases include pepsins, cathepsins, and renins. Two-domain structure, probably arising from ancestral duplication. This family does not include the retroviral nor retrotransposon proteases (Pfam:PF00077), which are much smaller and appear to be homologous to a single domain of the eukaryotic asp proteases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Procardosin-B,Procardosin-B	aspartic-type peptidase activity peptidase activity catalytic activity, acting on a protein hydrolase activity aspartic-type endopeptidase activity catalytic activity endopeptidase activity	primary metabolic process metabolic process cellular process lipid metabolic process proteolysis protein metabolic process macromolecule metabolic process	cellular anatomical structure membrane extracellular region membrane-bounded organelle storage vacuole intracellular anatomical structure vacuole intracellular membrane-bounded organelle protein storage vacuole intracellular organelle organelle plant-type vacuole cytoplasm lytic vacuole cellular anatomical structure membrane extracellular region membrane-bounded organelle storage vacuole intracellular anatomical structure vacuole intracellular membrane-bounded organelle protein storage vacuole intracellular organelle organelle plant-type vacuole cytoplasm lytic vacuole lysosome endoplasmic reticulum endomembrane system

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR033869	Phytepsin	Domain
A, B	IPR011001	Saposin-like	Homologous Superfamily
A, B	IPR007856	Saposin-like type B, region 1	Domain
A, B	IPR008139	Saposin B type domain	Domain
A, B	IPR001461	Aspartic peptidase A1	Family
A, B	IPR033121	Peptidase family A1 domain	Domain
A, B	IPR008138	Saposin B type, region 2	Domain
A, B	IPR021109	Aspartic peptidase domain superfamily	Homologous Superfamily
A, B	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.