8J47

CryoEM Structure of 40-Residue Arctic (E22G) Beta-Amyloid Fibril Derived by Co-Analysis with Solid-State NMR | E22G Abeta40

External Resource: Annotation

Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], F [auth A], G [auth H], H [auth G], I [auth J], J [auth I]	E22G Amyloid-beta	heparin binding glycosaminoglycan binding binding carbohydrate derivative binding sulfur compound binding	-	membrane-bounded organelle intracellular anatomical structure early endosome endosome intracellular vesicle intracellular membrane-bounded organelle endomembrane system intracellular organelle cellular anatomical structure cytoplasmic vesicle organelle cytoplasm vesicle somatodendritic compartment membrane-bounded organelle intracellular anatomical structure early endosome endosome intracellular vesicle intracellular membrane-bounded organelle endomembrane system intracellular organelle cellular anatomical structure cytoplasmic vesicle organelle cytoplasm vesicle somatodendritic compartment cell body perikaryon neuronal cell body clathrin-coated pit membrane extracellular region Golgi-associated vesicle cell surface cell periphery plasma membrane growth cone axon cell projection distal axon neuron projection plasma membrane bounded cell projection site of polarized growth nucleus

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], F [auth A], G [auth H], H [auth G], I [auth J], J [auth I]	IPR019543	Beta-amyloid precursor protein C-terminal	Domain
A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], F [auth A], G [auth H], H [auth G], I [auth J], J [auth I]	IPR036176	E2 domain superfamily	Homologous Superfamily
A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], F [auth A], G [auth H], H [auth G], I [auth J], J [auth I]	IPR013803	Amyloidogenic glycoprotein, amyloid-beta peptide	Domain
A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], F [auth A], G [auth H], H [auth G], I [auth J], J [auth I]	IPR019745	Amyloidogenic glycoprotein, intracellular domain, conserved site	Conserved Site
A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], F [auth A], G [auth H], H [auth G], I [auth J], J [auth I]	IPR037071	Amyloidogenic glycoprotein, amyloid-beta peptide superfamily	Homologous Superfamily
A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], F [auth A], G [auth H], H [auth G], I [auth J], J [auth I]	IPR024329	Amyloidogenic glycoprotein, E2 domain	Domain
A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], F [auth A], G [auth H], H [auth G], I [auth J], J [auth I]	IPR011993	PH-like domain superfamily	Homologous Superfamily
A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], A [auth D], B [auth C], C [auth F], D [auth E], E [auth B], F [auth A], G [auth H], H [auth G], I [auth J], J [auth I]	IPR008155	Amyloidogenic glycoprotein	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.