1UW3 | pdb_00001uw3

The crystal structure of the globular domain of sheep prion protein

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	d1uw3a_	Alpha and beta proteins (a+b)	Prion-like	Prion-like	Prion-like	Prion protein domain	(Ovis aries ) [TaxId: 9940 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Prion-like	8022803	4000908	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Prion-like	8035183	3001941	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	Prion	e1uw3A1	A: a+b two layers	X: Prion-like (From Topology)	H: Prion-like (From Topology)	T: Prion-like	F: Prion	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.790.10	Mainly Alpha	Orthogonal Bundle	Major Prion Protein	Prion/Doppel protein, beta-ribbon domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00377	Prion/Doppel alpha-helical domain (Prion)	Prion/Doppel alpha-helical domain	The prion protein is thought to be the infectious agent that causes transmissible spongiform encephalopathies, such as scrapie and BSE. It is thought that the prion protein can exist in two different forms: one is the normal cellular protein, and the ...	The prion protein is thought to be the infectious agent that causes transmissible spongiform encephalopathies, such as scrapie and BSE. It is thought that the prion protein can exist in two different forms: one is the normal cellular protein, and the other is the infectious form which can change the normal prion protein into the infectious form. It has been found that the prion alpha-helical domain is also found in the Doppel protein.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PRION PROTEIN	cation binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding cytoskeletal protein binding microtubule binding protein binding tubulin binding identical protein binding	cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein complex oligomerization protein-containing complex assembly protein homooligomerization cellular process cellular component organization or biogenesis	cellular anatomical structure membrane side of membrane cell periphery plasma membrane membrane-bounded organelle intracellular organelle intracellular anatomical structure Golgi apparatus organelle cytoplasm intracellular membrane-bounded organelle endomembrane system

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036924	Prion/Doppel beta-ribbon domain superfamily	Homologous Superfamily
A	IPR000817	Prion protein	Family
A	IPR025860	Major prion protein N-terminal	Domain
A	IPR022416	Prion/Doppel protein, beta-ribbon domain	Domain

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.