Annotations: 1O6E

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1o6ea_	All beta proteins	Herpes virus serine proteinase, assemblin	Herpes virus serine proteinase, assemblin	Herpes virus serine proteinase, assemblin	Epstein-Barr virus protease	HUMAN HERPESVIRUS 4 (human gammaherpesvirus 4 ) [TaxId: 10376 ],	SCOPe (2.08)
B	d1o6eb_	All beta proteins	Herpes virus serine proteinase, assemblin	Herpes virus serine proteinase, assemblin	Herpes virus serine proteinase, assemblin	Epstein-Barr virus protease	HUMAN HERPESVIRUS 4 (human gammaherpesvirus 4 ) [TaxId: 10376 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Herpes virus serine proteinase, assemblin	8044059	3001295	SCOP2B (2022-06-29)
B	SCOP2 Family	Herpes virus serine proteinase, assemblin	8031681	4002472	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Herpes virus serine proteinase, assemblin	8044059	3001295	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_S21	e1o6eA1	A: beta barrels	X: Herpes virus serine proteinase, assemblin (From Topology)	H: Herpes virus serine proteinase, assemblin (From Topology)	T: Herpes virus serine proteinase, assemblin	F: Peptidase_S21	ECOD (1.6)
B	Peptidase_S21	e1o6eB1	A: beta barrels	X: Herpes virus serine proteinase, assemblin (From Topology)	H: Herpes virus serine proteinase, assemblin (From Topology)	T: Herpes virus serine proteinase, assemblin	F: Peptidase_S21	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.16.10	Alpha Beta	Alpha-Beta Barrel	Serine Protease, Human Cytomegalovirus Protease	Chain A	CATH (4.3.0)
B	3.20.16.10	Alpha Beta	Alpha-Beta Barrel	Serine Protease, Human Cytomegalovirus Protease	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00716	Assemblin (Peptidase family S21) (Peptidase_S21)	Assemblin (Peptidase family S21)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	CAPSID PROTEIN P40	peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity identical protein binding protein binding binding	virion assembly viral process viral capsid assembly viral life cycle nuclear capsid assembly proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process exit from host cell biological process involved in interspecies interaction between organisms viral release from host cell biological process involved in interaction with host virion assembly viral process viral capsid assembly viral life cycle nuclear capsid assembly proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process exit from host cell biological process involved in interspecies interaction between organisms viral release from host cell biological process involved in interaction with host biological process involved in symbiotic interaction	host intracellular membrane-bounded organelle host cellular component host intracellular part host cell part host intracellular region cellular anatomical entity host cell nucleus host intracellular organelle host cell cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR035443	Herpesvirus protease superfamily	Homologous Superfamily
A, B	IPR001847	Peptidase S21	Family

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.