5H0Z

Crystal structure of P113A mutated human transthyretin

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue SO4 A 201

Chain	Residue
A	SER10
A	HIS56
A	GLY57
A	ARG104
A	HOH309

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site_id	AC2
Number of Residues	2
Details	binding site for residue CL A 202

Chain	Residue
A	LYS76
A	LYS80

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT

Chain	Residue	Details
A	LYS15
A	GLU54
A	SER117

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012

Chain	Residue	Details
A	GLU42

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02767

Chain	Residue	Details
A	SER52

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site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329

Chain	Residue	Details
A	ASN98

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