9CM9

Cryo-EM model derived from localized reconstruction of Ad657-hexon-FX complex at 3.86A resolution

External Resource: Annotation

Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth J], B [auth K], C [auth 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 [auth J], B [auth K], C [auth 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
D [auth Z]	PF00008	EGF-like domain (EGF)	EGF-like domain	There is no clear separation between noise and signal. Pfam:PF00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is t ...	There is no clear separation between noise and signal. Pfam:PF00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.	Domain
D [auth Z]	PF14670	Coagulation Factor Xa inhibitory site (FXa_inhibition)	Coagulation Factor Xa inhibitory site	This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442 [1].	Domain
D [auth Z]	PF00594	Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain (Gla)	Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain	This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).	Domain
D [auth Z]	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth J], B [auth K], C [auth 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 cellular component cellular anatomical structure host cell host intracellular membrane-bounded organelle host intracellular part host cell part host intracellular region host cell nucleus host intracellular organelle viral capsid icosahedral viral capsid virion component T=25 icosahedral viral capsid
D [auth Z]	Coagulation factor X	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding 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	multicellular organismal process regulation of body fluid levels wound healing response to stimulus hemostasis biological regulation blood coagulation response to stress coagulation regulation of biological quality response to wounding proteolysis metabolic process cellular process multicellular organismal process regulation of body fluid levels wound healing response to stimulus hemostasis biological regulation blood coagulation response to stress coagulation regulation of biological quality response to wounding proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	membrane-bounded organelle intracellular anatomical structure Golgi apparatus membrane-enclosed lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen Golgi lumen intracellular organelle cellular anatomical structure organelle lumen organelle cytoplasm endoplasmic reticulum lumen membrane-bounded organelle intracellular anatomical structure Golgi apparatus membrane-enclosed lumen intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen Golgi lumen intracellular organelle cellular anatomical structure organelle lumen organelle cytoplasm endoplasmic reticulum lumen endoplasmic reticulum extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth J], B [auth K], C [auth L]	IPR044942	Adenovirus Pll, hexon, subdomain 2	Homologous Superfamily
A [auth J], B [auth K], C [auth L]	IPR016107	Adenovirus Pll, hexon, N-terminal	Domain
A [auth J], B [auth K], C [auth L]	IPR016108	Adenovirus Pll, hexon, C-terminal	Domain
A [auth J], B [auth K], C [auth L]	IPR016112	Group II dsDNA virus coat/capsid protein	Homologous Superfamily
A [auth J], B [auth K], C [auth L]	IPR037542	Adenovirus hexon protein	Family
D [auth Z]	IPR050442	Peptidase S1 family, coagulation factors	Family
D [auth Z]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
D [auth Z]	IPR000294	Gamma-carboxyglutamic acid-rich (GLA) domain	Domain
D [auth Z]	IPR017857	Coagulation factor-like, Gla domain superfamily	Homologous Superfamily
D [auth Z]	IPR018097	EGF-like calcium-binding, conserved site	Conserved Site
D [auth Z]	IPR001314	Peptidase S1A, chymotrypsin family	Family
D [auth Z]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
D [auth Z]	IPR001254	Serine proteases, trypsin domain	Domain
D [auth Z]	IPR035972	Gamma-carboxyglutamic acid-rich (GLA) domain superfamily	Homologous Superfamily
D [auth Z]	IPR001881	EGF-like calcium-binding domain	Domain
D [auth Z]	IPR000742	EGF-like domain	Domain
D [auth Z]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
D [auth Z]	IPR000152	EGF-type aspartate/asparagine hydroxylation site	PTM
D [auth Z]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
D [auth Z]	IPR012224	Peptidase S1A, coagulation factor VII/IX/X/C/Z	Family