1SOQ

Crystal structure of the transthyretin mutant A108Y/L110E solved in space group C2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001523	biological_process	retinoid metabolic process
A	0003105	biological_process	negative regulation of glomerular filtration
A	0005179	molecular_function	hormone activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0006144	biological_process	purine nucleobase metabolic process
A	0007603	biological_process	phototransduction, visible light
A	0032991	cellular_component	protein-containing complex
A	0035578	cellular_component	azurophil granule lumen
A	0042562	molecular_function	hormone binding
A	0042802	molecular_function	identical protein binding
A	0044877	molecular_function	protein-containing complex binding
A	0070062	cellular_component	extracellular exosome
A	0140313	molecular_function	molecular sequestering activity
B	0001523	biological_process	retinoid metabolic process
B	0003105	biological_process	negative regulation of glomerular filtration
B	0005179	molecular_function	hormone activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0006144	biological_process	purine nucleobase metabolic process
B	0007603	biological_process	phototransduction, visible light
B	0032991	cellular_component	protein-containing complex
B	0035578	cellular_component	azurophil granule lumen
B	0042562	molecular_function	hormone binding
B	0042802	molecular_function	identical protein binding
B	0044877	molecular_function	protein-containing complex binding
B	0070062	cellular_component	extracellular exosome
B	0140313	molecular_function	molecular sequestering activity
C	0001523	biological_process	retinoid metabolic process
C	0003105	biological_process	negative regulation of glomerular filtration
C	0005179	molecular_function	hormone activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005737	cellular_component	cytoplasm
C	0006144	biological_process	purine nucleobase metabolic process
C	0007603	biological_process	phototransduction, visible light
C	0032991	cellular_component	protein-containing complex
C	0035578	cellular_component	azurophil granule lumen
C	0042562	molecular_function	hormone binding
C	0042802	molecular_function	identical protein binding
C	0044877	molecular_function	protein-containing complex binding
C	0070062	cellular_component	extracellular exosome
C	0140313	molecular_function	molecular sequestering activity
D	0001523	biological_process	retinoid metabolic process
D	0003105	biological_process	negative regulation of glomerular filtration
D	0005179	molecular_function	hormone activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005737	cellular_component	cytoplasm
D	0006144	biological_process	purine nucleobase metabolic process
D	0007603	biological_process	phototransduction, visible light
D	0032991	cellular_component	protein-containing complex
D	0035578	cellular_component	azurophil granule lumen
D	0042562	molecular_function	hormone binding
D	0042802	molecular_function	identical protein binding
D	0044877	molecular_function	protein-containing complex binding
D	0070062	cellular_component	extracellular exosome
D	0140313	molecular_function	molecular sequestering activity

Functional Information from PROSITE/UniProt

site_id	PS00768
Number of Residues	16
Details	TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV

Chain	Residue	Details
A	LYS15-VAL30

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11418763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ICT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"Sulfocysteine","evidences":[{"source":"PubMed","id":"17175208","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2H4E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"4-carboxyglutamate; in a patient with Moyamoya disease","evidences":[{"source":"PubMed","id":"18221012","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P02767","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19167329","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---