Annotations: 1EM9

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1em9a_	All alpha proteins	Retrovirus capsid protein, N-terminal core domain	Retrovirus capsid protein, N-terminal core domain	Retrovirus capsid protein, N-terminal core domain	RSV capsid protein	(Rous sarcoma virus - Prague C ) [TaxId: 11888 ],	SCOPe (2.08)
B	d1em9b_	All alpha proteins	Retrovirus capsid protein, N-terminal core domain	Retrovirus capsid protein, N-terminal core domain	Retrovirus capsid protein, N-terminal core domain	RSV capsid protein	(Rous sarcoma virus - Prague C ) [TaxId: 11888 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Retrovirus capsid protein, N-terminal core domain	8025494	4001095	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Retrovirus capsid protein, N-terminal core domain	8037873	3000745	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Retrovirus capsid protein, N-terminal core domain	8037873	3000745	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	Gag_p24_like	e1em9A1	A: alpha bundles	X: Retrovirus capsid protein	H: Retrovirus capsid protein N-terminal domain (From Topology)	T: Retrovirus capsid protein N-terminal domain	F: Gag_p24_like	ECOD (1.6)
B	Gag_p24_like	e1em9B1	A: alpha bundles	X: Retrovirus capsid protein	H: Retrovirus capsid protein N-terminal domain (From Topology)	T: Retrovirus capsid protein N-terminal domain	F: Gag_p24_like	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.375.10	Mainly Alpha	Orthogonal Bundle	Human Immunodeficiency Virus Type 1 Capsid Protein	Human Immunodeficiency Virus Type 1 Capsid Protein	CATH (4.3.0)
B	1.10.375.10	Mainly Alpha	Orthogonal Bundle	Human Immunodeficiency Virus Type 1 Capsid Protein	Human Immunodeficiency Virus Type 1 Capsid Protein	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00607	gag protein p24 N-terminal domain (Gag_p24)	gag protein p24 N-terminal domain	p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	GAG POLYPROTEIN CAPSID PROTEIN P27	binding nucleic acid binding aspartic-type peptidase activity peptidase activity catalytic activity, acting on a protein hydrolase activity aspartic-type endopeptidase activity catalytic activity endopeptidase activity structural constituent of virion structural molecule activity cation binding transition metal ion binding zinc ion binding binding nucleic acid binding aspartic-type peptidase activity peptidase activity catalytic activity, acting on a protein hydrolase activity aspartic-type endopeptidase activity catalytic activity endopeptidase activity structural constituent of virion structural molecule activity cation binding transition metal ion binding zinc ion binding ion binding metal ion binding small molecule binding	virus maturation viral life cycle viral capsid assembly viral procapsid maturation cellular component biogenesis cellular component organization virion assembly cellular component assembly viral process cellular process cellular component organization or biogenesis viral gene expression viral translational frameshifting viral translation virus maturation viral life cycle viral capsid assembly viral procapsid maturation cellular component biogenesis cellular component organization virion assembly cellular component assembly viral process cellular process cellular component organization or biogenesis viral gene expression viral translational frameshifting viral translation proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	host intracellular membrane-bounded organelle host cellular component host intracellular part cellular anatomical structure host cell part host intracellular region host cell nucleus host cell nucleolus host cell nuclear part host intracellular organelle membrane viral capsid virion component host cell plasma membrane host intracellular membrane-bounded organelle host cellular component host intracellular part cellular anatomical structure host cell part host intracellular region host cell nucleus host cell nucleolus host cell nuclear part host intracellular organelle membrane viral capsid virion component host cell plasma membrane host cell membrane host cell nucleoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR050195	Primate lentivirus group Gag polyprotein-like	Domain
A, B	IPR001995	Peptidase A2A, retrovirus, catalytic	Domain
A, B	IPR001878	Zinc finger, CCHC-type	Domain
A, B	IPR008919	Retrovirus capsid, N-terminal	Homologous Superfamily
A, B	IPR010999	Retroviral matrix protein	Homologous Superfamily
A, B	IPR012344	Matrix protein, lentiviral and alpha-retroviral, N-terminal	Homologous Superfamily
A, B	IPR021109	Aspartic peptidase domain superfamily	Homologous Superfamily
A, B	IPR001969	Aspartic peptidase, active site	Active Site
A, B	IPR018061	Retropepsins	Domain
A, B	IPR004028	Retroviral Gag polyprotein, M	Domain
A, B	IPR036875	Zinc finger, CCHC-type superfamily	Homologous Superfamily
A, B	IPR034170	Retropepsin-like catalytic domain	Domain
A, B	IPR008916	Retrovirus capsid, C-terminal	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.