4L1R

Glycoprotein B from Herpes Simplex Virus type 1, A549T Rate-of-Entry mutant, low-pH

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4l1ra_	Multi-domain proteins (alpha and beta)	Viral glycoprotein ectodomain-like	Viral glycoprotein ectodomain-like	Glycoprotein B-like	Glycoprotein B	HHV-1 (Human alphaherpesvirus 1 strain KOS ) [TaxId: 10306 ],	SCOPe (2.08)
B	d4l1rb_	Multi-domain proteins (alpha and beta)	Viral glycoprotein ectodomain-like	Viral glycoprotein ectodomain-like	Glycoprotein B-like	Glycoprotein B	HHV-1 (Human alphaherpesvirus 1 strain KOS ) [TaxId: 10306 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Viral glycoprotein ectodomain-like	8034129	3001498	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Viral glycoprotein ectodomain-like	8034129	3001498	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	PF17416	e4l1rA3	A: beta barrels	X: PH domain-like	H: first barrel domain in viral glycoproteins (From Topology)	T: first barrel domain in viral glycoproteins	F: PF17416	ECOD (1.6)
A	PF17417	e4l1rA2	A: beta barrels	X: PH domain-like	H: second barrel domain in viral glycoproteins (From Topology)	T: second barrel domain in viral glycoproteins	F: PF17417	ECOD (1.6)
A	PF00606	e4l1rA1	A: beta complex topology	X: Viral glycoprotein ectodomain-like (From Topology)	H: Viral glycoprotein ectodomain-like (From Topology)	T: Viral glycoprotein ectodomain-like	F: PF00606	ECOD (1.6)
B	PF17416	e4l1rB8	A: beta barrels	X: PH domain-like	H: first barrel domain in viral glycoproteins (From Topology)	T: first barrel domain in viral glycoproteins	F: PF17416	ECOD (1.6)
B	PF17417	e4l1rB9	A: beta barrels	X: PH domain-like	H: second barrel domain in viral glycoproteins (From Topology)	T: second barrel domain in viral glycoproteins	F: PF17417	ECOD (1.6)
B	PF00606	e4l1rB7	A: beta complex topology	X: Viral glycoprotein ectodomain-like (From Topology)	H: Viral glycoprotein ectodomain-like (From Topology)	T: Viral glycoprotein ectodomain-like	F: PF00606	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.30.30.1230	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
A	1.20.5.1890	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
A	2.30.29.100	Mainly Beta	Roll	PH-domain like		CATH (4.3.0)
A	6.10.250.3280	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
B	2.30.30.1230	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)
B	1.20.5.1890	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
B	2.30.29.100	Mainly Beta	Roll	PH-domain like		CATH (4.3.0)
B	6.10.250.3280	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00606	Herpesvirus Glycoprotein B ectodomain (Glycoprotein_B)	Herpesvirus Glycoprotein B ectodomain	This domain corresponds to the ectodomain of glycoprotein B according to ECOD.	Domain
A, B	PF17417	Herpesvirus Glycoprotein B PH-like domain (Glycoprot_B_PH2)	Herpesvirus Glycoprotein B PH-like domain	This domain corresponds to the second PH-like domain in herpesvirus glycoprotein B.	Domain
A, B	PF17416	Herpesvirus Glycoprotein B (Glycoprot_B_PH1)	Herpesvirus Glycoprotein B	This domain has a PH-like fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Envelope glycoprotein B	identical protein binding protein binding binding	virion attachment to host cell biological process involved in interspecies interaction between organisms adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host biological process involved in interaction with host biological process involved in symbiotic interaction symbiont entry into host cell symbiont entry into host	membrane cellular anatomical entity virion component virion membrane host intracellular membrane-bounded organelle host cellular component host intracellular part host cell membrane host cell cytoplasm part host intracellular organelle host cell endosome membrane host cell cytoplasm host cell part host cell endosome membrane cellular anatomical entity virion component virion membrane host intracellular membrane-bounded organelle host cellular component host intracellular part host cell membrane host cell cytoplasm part host intracellular organelle host cell endosome membrane host cell cytoplasm host cell part host cell endosome host intracellular region viral membrane viral envelope host cell plasma membrane host cell Golgi membrane host cell Golgi apparatus host cell endomembrane system

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR035381	Herpesvirus Glycoprotein B, PH-like domain 2	Domain
A, B	IPR035377	Herpesvirus Glycoprotein B, PH-like domain 1	Domain
A, B	IPR000234	Herpesvirus Glycoprotein B	Family
A, B	IPR038631	Herpesvirus Glycoprotein B, PH-like domain 2 superfamily	Homologous Superfamily

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.