2CEO

thyroxine-binding globulin complex with thyroxine

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d2ceob_	Multi-domain proteins (alpha and beta)	Serpins	Serpins	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2ceoa_	Multi-domain proteins (alpha and beta)	Serpins	Serpins	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Serpins	8070175	3001563	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Serpins	8070175	3001563	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)
B	Serpin	e2ceoB1	A: a+b complex topology	X: Serpins (From Topology)	H: Serpins (From Topology)	T: Serpins	F: Serpin	ECOD (1.6)
A	Serpin	e2ceoA1	A: a+b complex topology	X: Serpins (From Topology)	H: Serpins (From Topology)	T: Serpins	F: Serpin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.497.10	Alpha Beta	2-Layer Sandwich	Antithrombin	Chain I, domain 2	CATH (4.3.0)
B	2.30.39.10	Mainly Beta	Roll	Alpha-1-antitrypsin	domain 1	CATH (4.3.0)
A	3.30.497.10	Alpha Beta	2-Layer Sandwich	Antithrombin	Chain I, domain 2	CATH (4.3.0)
A	2.30.39.10	Mainly Beta	Roll	Alpha-1-antitrypsin	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00079	Serpin (serine protease inhibitor) (Serpin)	Serpin (serine protease inhibitor)	Structure is a multi-domain fold containing a bundle of helices and a beta sandwich.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	THYROXINE-BINDING GLOBULIN	enzyme regulator activity molecular function inhibitor activity peptidase regulator activity serine-type endopeptidase inhibitor activity molecular function regulator activity enzyme inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity	thyroid hormone transport localization transport regulation of hormone levels biological regulation hormone transport regulation of biological quality establishment of localization	cellular anatomical structure extracellular region extracellular space extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle vesicle extracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR042178	Serpin superfamily, domain 1	Homologous Superfamily
A, B	IPR023795	Serpin, conserved site	Conserved Site
A, B	IPR042185	Serpin superfamily, domain 2	Homologous Superfamily
A, B	IPR036186	Serpin superfamily	Homologous Superfamily
A, B	IPR000215	Serpin family	Family
A, B	IPR023796	Serpin domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P05543	inborn errors of metabolism Liver Cirrhosis, Experimental hyperthyroidism hyperthyroxinemia hypothyroidism pancreatic ductal adenocarcinoma

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.