Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1ICT

MONOCLINIC FORM OF HUMAN TRANSTHYRETIN COMPLEXED WITH THYROXINE (T4)

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0007165	biological_process	signal transduction
A	0035578	cellular_component	azurophil granule lumen
A	0042802	molecular_function	identical protein binding
A	0070062	cellular_component	extracellular exosome
A	0070324	molecular_function	thyroid hormone binding
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	0007165	biological_process	signal transduction
B	0035578	cellular_component	azurophil granule lumen
B	0042802	molecular_function	identical protein binding
B	0070062	cellular_component	extracellular exosome
B	0070324	molecular_function	thyroid hormone binding
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	0007165	biological_process	signal transduction
C	0035578	cellular_component	azurophil granule lumen
C	0042802	molecular_function	identical protein binding
C	0070062	cellular_component	extracellular exosome
C	0070324	molecular_function	thyroid hormone binding
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	0007165	biological_process	signal transduction
D	0035578	cellular_component	azurophil granule lumen
D	0042802	molecular_function	identical protein binding
D	0070062	cellular_component	extracellular exosome
D	0070324	molecular_function	thyroid hormone binding
E	0005179	molecular_function	hormone activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0005737	cellular_component	cytoplasm
E	0006144	biological_process	purine nucleobase metabolic process
E	0007165	biological_process	signal transduction
E	0035578	cellular_component	azurophil granule lumen
E	0042802	molecular_function	identical protein binding
E	0070062	cellular_component	extracellular exosome
E	0070324	molecular_function	thyroid hormone binding
F	0005179	molecular_function	hormone activity
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005615	cellular_component	extracellular space
F	0005737	cellular_component	cytoplasm
F	0006144	biological_process	purine nucleobase metabolic process
F	0007165	biological_process	signal transduction
F	0035578	cellular_component	azurophil granule lumen
F	0042802	molecular_function	identical protein binding
F	0070062	cellular_component	extracellular exosome
F	0070324	molecular_function	thyroid hormone binding
G	0005179	molecular_function	hormone activity
G	0005515	molecular_function	protein binding
G	0005576	cellular_component	extracellular region
G	0005615	cellular_component	extracellular space
G	0005737	cellular_component	cytoplasm
G	0006144	biological_process	purine nucleobase metabolic process
G	0007165	biological_process	signal transduction
G	0035578	cellular_component	azurophil granule lumen
G	0042802	molecular_function	identical protein binding
G	0070062	cellular_component	extracellular exosome
G	0070324	molecular_function	thyroid hormone binding
H	0005179	molecular_function	hormone activity
H	0005515	molecular_function	protein binding
H	0005576	cellular_component	extracellular region
H	0005615	cellular_component	extracellular space
H	0005737	cellular_component	cytoplasm
H	0006144	biological_process	purine nucleobase metabolic process
H	0007165	biological_process	signal transduction
H	0035578	cellular_component	azurophil granule lumen
H	0042802	molecular_function	identical protein binding
H	0070062	cellular_component	extracellular exosome
H	0070324	molecular_function	thyroid hormone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE T44 C 128

Chain	Residue
A	LYS15
C	ALA108
C	SER117
C	THR119
C	VAL121
A	LEU17
A	ALA108
A	ALA109
A	LEU110
A	SER117
C	LYS15
C	LEU17
C	GLU54

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE T44 D 129

Chain	Residue
B	LYS15
B	LEU17
B	LEU110
B	SER117
B	THR118
B	THR119
D	LYS15
D	LEU17
D	THR106
D	LEU110
D	SER117
D	THR119
D	VAL121

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

site_id	PS00769
Number of Residues	13
Details	TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS

Chain	Residue	Details
A	TYR105-SER117

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:11418763, ECO:0007744\|PDB:1ICT

Chain	Residue	Details
A	LYS15
D	LYS15
D	GLU54
D	SER117
E	LYS15
E	GLU54
E	SER117
F	LYS15
F	GLU54
F	SER117
G	LYS15
A	GLU54
G	GLU54
G	SER117
H	LYS15
H	GLU54
H	SER117
A	SER117
B	LYS15
B	GLU54
B	SER117
C	LYS15
C	GLU54
C	SER117

site_id	SWS_FT_FI2
Number of Residues	8
Details	MOD_RES: Sulfocysteine => ECO:0000269\|PubMed:17175208, ECO:0007744\|PDB:2H4E

Chain	Residue	Details
A	CYS10
B	CYS10
C	CYS10
D	CYS10
E	CYS10
F	CYS10
G	CYS10
H	CYS10

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269\|PubMed:18221012

Chain	Residue	Details
A	GLU42
B	GLU42
C	GLU42
D	GLU42
E	GLU42
F	GLU42
G	GLU42
H	GLU42

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P02767

Chain	Residue	Details
A	SER52
B	SER52
C	SER52
D	SER52
E	SER52
F	SER52
G	SER52
H	SER52

site_id	SWS_FT_FI5
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:19167329

Chain	Residue	Details
A	ASN98
B	ASN98
C	ASN98
D	ASN98
E	ASN98
F	ASN98
G	ASN98
H	ASN98

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)