3ZIF

Cryo-EM structures of two intermediates provide insight into adenovirus assembly and disassembly

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	PF01065	e3zifB1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
B	PF03678	e3zifB2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
C	PF01065	e3zifC1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
C	PF03678	e3zifC2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
D	PF01065	e3zifD1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
D	PF03678	e3zifD2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
F	PF01065	e3zifF1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
F	PF03678	e3zifF2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
I	PF01065	e3zifI1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
I	PF03678	e3zifI2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
L	PF01065	e3zifL1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
L	PF03678	e3zifL2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
A	PF01065	e3zifA1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
A	PF03678	e3zifA2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
E	PF01065	e3zifE1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
E	PF03678	e3zifE2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
G	PF01065	e3zifG1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
G	PF03678	e3zifG2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
H	PF01065	e3zifH1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
H	PF03678	e3zifH2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
J	PF01065	e3zifJ1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
J	PF03678	e3zifJ2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
K	PF01065	e3zifK1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF01065	ECOD (1.6)
K	PF03678	e3zifK2	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF03678	ECOD (1.6)
M	PF01686	e3zifM1	A: beta sandwiches	X: jelly-roll	H: Jelly-roll domain in Adenovirus penton base protein (From Topology)	T: Jelly-roll domain in Adenovirus penton base protein	F: PF01686	ECOD (1.6)
M	PF01686	e3zifM2	A: a+b complex topology	X: Insertion domain in Adenovirus penton base protein (From Topology)	H: Insertion domain in Adenovirus penton base protein (From Topology)	T: Insertion domain in Adenovirus penton base protein	F: PF01686	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	PF01065	Hexon, adenovirus major coat protein, N-terminal domain (Adeno_hexon)	Hexon, adenovirus major coat protein, N-terminal domain	Hexon is the major coat protein from adenovirus type 2. Hexon forms a homo-trimer. The 240 copies of the hexon trimer are organised so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polype ...	Hexon is the major coat protein from adenovirus type 2. Hexon forms a homo-trimer. The 240 copies of the hexon trimer are organised so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polypeptide IX. The penton complex, formed by the peripentonal hexons and base hexon (holding in place a fibre), lie at each of the 12 vertices [1]. The N and C-terminal domains adopt the same PNGase F-like fold although they are significantly different in length.	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	PF03678	Hexon, adenovirus major coat protein, C-terminal domain (Adeno_hexon_C)	Hexon, adenovirus major coat protein, C-terminal domain	Hexon is the major coat protein from adenovirus type 2. Hexon forms a homo-trimer. The 240 copies of the hexon trimer are organised so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polype ...	Hexon is the major coat protein from adenovirus type 2. Hexon forms a homo-trimer. The 240 copies of the hexon trimer are organised so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polypeptide IX. The penton complex, formed by the peripentonal hexons and base hexon (holding in place a fibre), lie at each of the 12 vertices [1]. The N and C-terminal domains adopt the same PNGase F-like fold although they are significantly different in length.	Domain
N, O, P, Q	PF03955	Adenovirus hexon-associated protein (IX) (Adeno_PIX)	Adenovirus hexon-associated protein (IX)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	HEXON PROTEIN	structural molecule activity	microtubule-dependent intracellular transport of viral material microtubule-dependent intracellular transport of viral material towards nucleus intracellular transport of virus viral process viral life cycle transport of virus transport of viral material towards nucleus biological process involved in interspecies interaction between organisms symbiont entry into host cell symbiont entry into host 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 viral capsid icosahedral viral capsid virion component T=25 icosahedral viral capsid
M	PENTON PROTEIN	-	-	-
N, O, P, Q	PIX	hexon binding protein binding binding	-	viral capsid virion component viral capsid, decoration
R	PVIII	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR044942	Adenovirus Pll, hexon, subdomain 2	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR016110	Adenovirus Pll, hexon, subdomain 3	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR016107	Adenovirus Pll, hexon, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR016108	Adenovirus Pll, hexon, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR016112	Group II dsDNA virus coat/capsid protein	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR037542	Adenovirus hexon protein	Family
N, O, P, Q	IPR005641	Hexon-associated protein IX	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 R01GM133198.

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3ZIF

Cryo-EM structures of two intermediates provide insight into adenovirus assembly and disassembly

External Resource: Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Protein Family Annotation Pfam Database Homepage

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

InterPro: Protein Family Classification InterPro Database Homepage