1GKO

An Engineered Transthyretin Monomer that is Non-amyloidogenic - Unless Partially Denatured

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)
A	d1gkoa_	All beta proteins	Prealbumin-like	Transthyretin (synonym: prealbumin)	Transthyretin (synonym: prealbumin)	Transthyretin (synonym: prealbumin)	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1gkoc_	All beta proteins	Prealbumin-like	Transthyretin (synonym: prealbumin)	Transthyretin (synonym: prealbumin)	Transthyretin (synonym: prealbumin)	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d1gkod_	All beta proteins	Prealbumin-like	Transthyretin (synonym: prealbumin)	Transthyretin (synonym: prealbumin)	Transthyretin (synonym: prealbumin)	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1gkob_	All beta proteins	Prealbumin-like	Transthyretin (synonym: prealbumin)	Transthyretin (synonym: prealbumin)	Transthyretin (synonym: prealbumin)	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)
A	SCOP2B Superfamily	Transthyretin (synonym: prealbumin)	8040289	3000848	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Transthyretin (synonym: prealbumin)	8040289	3000848	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Transthyretin (synonym: prealbumin)	8040289	3000848	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Transthyretin (synonym: prealbumin)	8040289	3000848	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)
A	Transthyretin	e1gkoA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Prealbumin-like	F: Transthyretin	ECOD (1.6)
C	Transthyretin	e1gkoC1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Prealbumin-like	F: Transthyretin	ECOD (1.6)
D	Transthyretin	e1gkoD1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Prealbumin-like	F: Transthyretin	ECOD (1.6)
B	Transthyretin	e1gkoB1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Prealbumin-like	F: Transthyretin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.180	Mainly Beta	Sandwich	Immunoglobulin-like	Transthyretin/hydroxyisourate hydrolase domain	CATH (4.3.0)
C	2.60.40.180	Mainly Beta	Sandwich	Immunoglobulin-like	Transthyretin/hydroxyisourate hydrolase domain	CATH (4.3.0)
D	2.60.40.180	Mainly Beta	Sandwich	Immunoglobulin-like	Transthyretin/hydroxyisourate hydrolase domain	CATH (4.3.0)
B	2.60.40.180	Mainly Beta	Sandwich	Immunoglobulin-like	Transthyretin/hydroxyisourate hydrolase domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00576	HIUase/Transthyretin family (Transthyretin)	HIUase/Transthyretin family	This family includes transthyretin that is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. However, most of the sequences listed in this family do not bind thyroid hormones. They are actually enzymes of ...	This family includes transthyretin that is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. However, most of the sequences listed in this family do not bind thyroid hormones. They are actually enzymes of the purine catabolism that catalyse the conversion of 5-hydroxyisourate (HIU) to OHCU [2,3]. HIU hydrolysis is the original function of the family and is conserved from bacteria to mammals; transthyretins arose by gene duplications in the vertebrate lineage [4]. HIUases are distinguished in the alignment from the conserved C-terminal YRGS sequence.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	TRANSTHYRETIN	hormone activity protein binding binding molecular function activator activity signaling receptor binding molecular function regulator activity signaling receptor regulator activity receptor ligand activity signaling receptor activator activity thyroid hormone binding hormone binding identical protein binding	nucleobase-containing compound metabolic process purine nucleobase metabolic process nucleobase-containing small molecule metabolic process nucleobase metabolic process small molecule metabolic process metabolic process cellular process primary metabolic process purine-containing compound metabolic process	cellular anatomical structure extracellular region extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure lytic vacuole intracellular vesicle membrane-enclosed lumen cellular anatomical structure extracellular region extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure lytic vacuole intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen vacuolar lumen endomembrane system intracellular organelle lumen intracellular organelle cytoplasmic vesicle lysosome vesicle lumen azurophil granule vacuole intracellular membrane-bounded organelle secretory granule lumen azurophil granule lumen organelle lumen secretory granule primary lysosome secretory vesicle cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036817	Transthyretin/hydroxyisourate hydrolase domain superfamily	Homologous Superfamily
A, B, C, D	IPR023418	Transthyretin, thyroxine binding site	Binding Site
A, B, C, D	IPR023419	Transthyretin, conserved site	Conserved Site
A, B, C, D	IPR023416	Transthyretin/hydroxyisourate hydrolase domain	Domain
A, B, C, D	IPR000895	Transthyretin/hydroxyisourate hydrolase	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P02766	amyloidosis familial amyloid neuropathy carpal tunnel syndrome hyperthyroxinemia, dystransthyretinemic lattice corneal dystrophy peripheral neuropathy Transthyretin related familial amyloid cardiomyopathy carpal tunnel syndrome 1 diabetes mellitus pancreatic intraductal papillary-mucinous carcinoma peripheral nervous system disease drug-induced liver injury Riley-Day syndrome acquired metabolic disease hydrocephalus amyloidosis familial amyloid neuropathy carpal tunnel syndrome hyperthyroxinemia, dystransthyretinemic lattice corneal dystrophy peripheral neuropathy Transthyretin related familial amyloid cardiomyopathy carpal tunnel syndrome 1 diabetes mellitus pancreatic intraductal papillary-mucinous carcinoma peripheral nervous system disease drug-induced liver injury Riley-Day syndrome acquired metabolic disease hydrocephalus intellectual disability Charcot-Marie-Tooth disease medulloblastoma osteosarcoma dilated cardiomyopathy pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia psoriasis schizophrenia acute kidney failure kidney disease lung benign neoplasm lymphatic system disease depressive disorder periodic fever syndrome polyneuropathy rheumatoid arthritis Sjogren syndrome heart disease hereditary amyloidosis hypertrophic cardiomyopathy lung carcinoma

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.