4DEU

Crystal Structure of the Wild Type TTR Binding Naringenin (TTRwt:NAR)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 201

Chain	Residue
A	PHE44
A	GLU66
A	ASP99
A	EDO202
A	HOH369
A	HOH410

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 202

Chain	Residue
A	HOH410
A	GLU66
A	ASP99
A	EDO201

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 203

Chain	Residue
A	SER23
A	PRO24
A	VAL122
A	THR123
A	EDO204
A	HOH384
A	HOH408

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 204

Chain	Residue
A	PRO24
A	ILE26
A	GLU51
A	EDO203
A	HOH357

---

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAR A 205

Chain	Residue
A	LYS15
A	LYS15
A	LEU17
A	LEU17
A	ALA108
A	ALA108
A	LEU110
A	SER117
A	THR119
A	THR119
A	HOH338
A	HOH338
A	HOH397
A	HOH404
A	HOH404
A	HOH411
A	HOH411
B	SER115

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 206

Chain	Residue
A	ARG34
A	SER46
A	GLY47
A	HIS56
A	GLU66
A	HOH311
A	HOH383

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 207

Chain	Residue
A	ASP74
A	LYS76
A	SER77
A	GLU89
A	HOH308
A	HOH319
A	HOH327

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 208

Chain	Residue
A	ALA37
A	LYS48
A	GLU54
A	LEU55
A	HIS56
A	HOH391

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 201

Chain	Residue
B	PHE44
B	ALA45
B	GLY57
B	LEU58
B	GLU63
B	GLU66
B	ASP99

---

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NAR B 202

Chain	Residue
B	LYS15
B	LYS15
B	LEU17
B	ALA108
B	ALA108
B	LEU110
B	SER117
B	THR119
B	THR119
B	VAL121
B	HOH393
B	HOH397
B	HOH407

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA B 203

Chain	Residue
B	SER46
B	ASN98

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 204

Chain	Residue
B	ARG34
B	LYS35
B	GLY67
B	ILE68

---

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 205

Chain	Residue
A	HIS90
A	GLU92
A	HOH375
B	TRP41
B	LYS70
B	GLU92
B	HOH338
B	HOH375

---

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	6
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	2
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	2
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	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P02767","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
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

---