Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GRB

Crystal structure of the F87M/L110M mutant of human transthyretin at pH 6.5

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001523	biological_process	retinoid metabolic process
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	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	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	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	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	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	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	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 PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 129

Chain	Residue
A	CYS10
A	HIS56
A	HOH153
A	HOH308

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 130

Chain	Residue
A	HIS88
A	HIS90
A	GLU92
A	HOH311

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 131

Chain	Residue
A	ALA36
A	ALA37
A	ARG34

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL A 132

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

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 133

Chain	Residue
A	LYS70
A	GLU72
A	GLU92
B	TRP41
B	LYS70
B	VAL94
B	HOH220

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 134

Chain	Residue
A	HIS31
A	GLU72
A	ASP74
A	HOH325

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 128

Chain	Residue
B	CYS10
B	HIS56
B	HOH312
B	HOH313

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

Chain	Residue
B	HIS31
B	GLU72
B	ASP74
B	HOH322

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

Chain	Residue
B	HIS88
B	HIS90
B	GLU92
B	HOH134

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 131

Chain	Residue
B	HIS31
B	SER46
B	GLY47

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

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

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 128

Chain	Residue
D	CYS10
D	HIS56
D	HOH136
D	HOH315

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

Chain	Residue
D	HIS88
D	HIS90
D	GLU92
D	HOH317

site_id	BC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ACT D 130

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	HOH159

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT D 131

Chain	Residue
D	GLY57
D	GLU63

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 132

Chain	Residue
C	TRP41
C	LYS70
C	VAL94
D	TRP41
D	LYS70
D	GLU72
D	GLU92

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 133

Chain	Residue
D	HIS31
D	GLU72
D	ASP74
D	HOH326

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL D 134

Chain	Residue
D	ARG34
D	ALA37

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

Chain	Residue
C	CYS10
C	HIS56
C	HOH318
C	HOH319

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

Chain	Residue
C	HIS90
C	GLU92
C	HOH137
C	HIS88

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT C 130

Chain	Residue
C	THR96
C	ASP99
C	TYR105
D	MET87
D	TYR114
D	HOH165

site_id	CC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ACT C 131

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

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 132

Chain	Residue
C	HIS31
C	SER46
C	GLY47

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 133

Chain	Residue
C	HIS31
C	GLU72
C	ASP74
C	HOH323

site_id	CC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACT C 134

Chain	Residue
B	MET110
B	SER115
B	SER117
C	SER115
C	TYR116
C	SER117
C	HOH171
C	HOH176

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 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

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