6Q2R

Cryo-EM structure of RET/GFRa2/NRTN extracellular complex in the tetrameric form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008083	molecular_function	growth factor activity
A	0030116	molecular_function	glial cell-derived neurotrophic factor receptor binding
A	0030971	molecular_function	receptor tyrosine kinase binding
B	0008083	molecular_function	growth factor activity
B	0030116	molecular_function	glial cell-derived neurotrophic factor receptor binding
B	0030971	molecular_function	receptor tyrosine kinase binding
C	0038023	molecular_function	signaling receptor activity
D	0038023	molecular_function	signaling receptor activity
E	0005509	molecular_function	calcium ion binding
E	0007156	biological_process	homophilic cell adhesion via plasma membrane adhesion molecules
E	0016020	cellular_component	membrane
F	0005509	molecular_function	calcium ion binding
F	0007156	biological_process	homophilic cell adhesion via plasma membrane adhesion molecules
F	0016020	cellular_component	membrane
U	0008083	molecular_function	growth factor activity
U	0030116	molecular_function	glial cell-derived neurotrophic factor receptor binding
U	0030971	molecular_function	receptor tyrosine kinase binding
V	0008083	molecular_function	growth factor activity
V	0030116	molecular_function	glial cell-derived neurotrophic factor receptor binding
V	0030971	molecular_function	receptor tyrosine kinase binding
W	0038023	molecular_function	signaling receptor activity
X	0038023	molecular_function	signaling receptor activity
Y	0005509	molecular_function	calcium ion binding
Y	0007156	biological_process	homophilic cell adhesion via plasma membrane adhesion molecules
Y	0016020	cellular_component	membrane
Z	0005509	molecular_function	calcium ion binding
Z	0007156	biological_process	homophilic cell adhesion via plasma membrane adhesion molecules
Z	0016020	cellular_component	membrane

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2424
Details	TOPO_DOM: Extracellular => ECO:0000255

Chain	Residue	Details
E	LEU29-ARG635
U	ARG158
U	ARG160
U	GLN162
V	ARG149
V	ARG158
V	ARG160
V	GLN162
F	LEU29-ARG635
Y	LEU29-ARG635
Z	LEU29-ARG635
W	ASN52
W	ASN357
X	ASN52
X	ASN357
U	ARG149

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site_id	SWS_FT_FI2
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269|PubMed:31535977, ECO:0000305|PubMed:25242331, ECO:0007744|PDB:4UX8, ECO:0007744|PDB:6Q2J

Chain	Residue	Details
E	GLU178
F	ASP230
F	ASP264
F	GLU265
F	ASP266
F	SER268
F	ASP300
F	ASP302
Y	GLU178
Y	ASP230
Y	ASP264
E	ASP230
Y	GLU265
Y	ASP266
Y	SER268
Y	ASP300
Y	ASP302
Z	GLU178
Z	ASP230
Z	ASP264
Z	GLU265
Z	ASP266
E	ASP264
Z	SER268
Z	ASP300
Z	ASP302
E	GLU265
E	ASP266
E	SER268
E	ASP300
E	ASP302
F	GLU178

---

site_id	SWS_FT_FI3
Number of Residues	40
Details	BINDING: BINDING => ECO:0000269|PubMed:31535977, ECO:0007744|PDB:6Q2J

Chain	Residue	Details
E	ASN179
E	ASP584
F	ASN179
F	GLU232
F	ASP267
F	ASP378
F	THR564
F	CYS565
F	ASP567
F	HIS569
F	GLU574
E	GLU232
F	ASP584
Y	ASN179
Y	GLU232
Y	ASP267
Y	ASP378
Y	THR564
Y	CYS565
Y	ASP567
Y	HIS569
Y	GLU574
E	ASP267
Y	ASP584
Z	ASN179
Z	GLU232
Z	ASP267
Z	ASP378
Z	THR564
Z	CYS565
Z	ASP567
Z	HIS569
Z	GLU574
E	ASP378
Z	ASP584
E	THR564
E	CYS565
E	ASP567
E	HIS569
E	GLU574

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site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Breakpoint for translocation to form the TRIM27/RET oncogene => ECO:0000269|PubMed:3037315

Chain	Residue	Details
E	ARG587
F	ARG587
Y	ARG587
Z	ARG587

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site_id	SWS_FT_FI5
Number of Residues	44
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
E	ASN98
E	ASN468
E	ASN554
F	ASN98
F	ASN199
F	ASN336
F	ASN343
F	ASN361
F	ASN367
F	ASN377
F	ASN394
E	ASN199
F	ASN448
F	ASN468
F	ASN554
Y	ASN98
Y	ASN199
Y	ASN336
Y	ASN343
Y	ASN361
Y	ASN367
Y	ASN377
E	ASN336
Y	ASN394
Y	ASN448
Y	ASN468
Y	ASN554
Z	ASN98
Z	ASN199
Z	ASN336
Z	ASN343
Z	ASN361
Z	ASN367
E	ASN343
Z	ASN377
Z	ASN394
Z	ASN448
Z	ASN468
Z	ASN554
E	ASN361
E	ASN367
E	ASN377
E	ASN394
E	ASN448

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site_id	SWS_FT_FI6
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20473317

Chain	Residue	Details
E	ASN151
F	ASN151
Y	ASN151
Z	ASN151

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