Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GRG

Crystal structure of the F87M/L110M mutant of human transthyretin at pH 7.5

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN A 129

Chain	Residue
A	CYS10
A	HIS56

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 130

Chain	Residue
A	HIS31
A	ASP74
A	HOH206

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 131

Chain	Residue
A	HOH209
A	HIS88
A	HIS90
A	GLU92
A	HOH208

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT A 132

Chain	Residue
A	TRP41
A	LYS70
A	GLU92
A	HOH168
B	TRP41
B	LYS70

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL A 133

Chain	Residue
A	THR75
A	TRP79
A	PRO86
A	MET87
A	HIS88
A	HIS90
A	SER112
A	PRO113
A	SER115
A	TYR116
A	HOH143

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A 134

Chain	Residue
A	ARG34
A	ALA36
A	ALA37

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 128

Chain	Residue
B	CYS10
B	HIS56
B	HOH210

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 129

Chain	Residue
B	HIS31
B	GLU72
B	ASP74
B	HOH134

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 130

Chain	Residue
B	HIS88
B	HIS90
B	GLU92
B	HOH133

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT B 131

Chain	Residue
B	THR75
B	TRP79
B	MET87
B	HIS88
B	HIS90
B	ALA91
B	SER112

site_id	BC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL B 132

Chain	Residue
B	ALA19
B	MET110
B	LEU111
B	SER112
B	SER115
B	TYR116
B	SER117
C	ALA19
C	MET110
C	SER112
C	SER117

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN D 128

Chain	Residue
D	CYS10
D	HIS56
D	HOH214

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 129

Chain	Residue
D	HIS31
D	ASP74
D	HOH215
D	HOH230

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 130

Chain	Residue
D	HIS88
D	HIS90
D	GLU92
D	HOH219

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ACT D 131

Chain	Residue
D	THR75
D	TRP79
D	PRO86
D	MET87
D	HIS88
D	HIS90
D	ALA91
D	SER112
D	PRO113
D	SER115
D	TYR116
D	HOH148

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT D 132

Chain	Residue
C	TRP41
C	LYS70
D	TRP41
D	LYS70
D	HOH136
D	HOH183

site_id	BC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GOL D 133

Chain	Residue
D	TYR116
D	SER117
A	ALA19
A	MET110
A	SER112
A	SER115
A	TYR116
A	SER117
D	ALA19
D	MET110
D	LEU111
D	SER112
D	SER115

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 134

Chain	Residue
D	ARG34
D	ALA36
D	ALA37

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 128

Chain	Residue
C	CYS10
C	HIS56
C	HOH220
C	HOH221

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 129

Chain	Residue
C	HIS31
C	GLU72
C	ASP74
C	HOH136

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 130

Chain	Residue
C	HIS88
C	HIS90
C	GLU92
C	HOH134

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT C 131

Chain	Residue
C	THR96
C	TYR105
C	HOH158
D	PRO86
D	MET87
D	TYR114

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACT C 132

Chain	Residue
C	THR75
C	TRP79
C	PRO86
C	HIS88
C	HIS90
C	SER112
C	SER115
C	TYR116

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. YTIAamLSPYSYS

Chain	Residue	Details
A	TYR105-SER117

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:11418763, ECO:0007744\|PDB:1ICT

Chain	Residue	Details
A	LYS15
C	LYS15
C	GLU54
C	SER117
A	GLU54
A	SER117
B	LYS15
B	GLU54
B	SER117
D	LYS15
D	GLU54
D	SER117

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: Sulfocysteine => ECO:0000269\|PubMed:17175208, ECO:0007744\|PDB:2H4E

Chain	Residue	Details
A	CYS10
B	CYS10
D	CYS10
C	CYS10

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

Chain	Residue	Details
A	GLU42
B	GLU42
D	GLU42
C	GLU42

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P02767

Chain	Residue	Details
A	SER52
B	SER52
D	SER52
C	SER52

site_id	SWS_FT_FI5
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:19167329

Chain	Residue	Details
A	ASN98
B	ASN98
D	ASN98
C	ASN98

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)