Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6Q2N

Cryo-EM structure of RET/GFRa1/GDNF extracellular complex

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	0001822	biological_process	kidney development
C	0005030	molecular_function	neurotrophin receptor activity
C	0005102	molecular_function	signaling receptor binding
C	0005178	molecular_function	integrin binding
C	0005576	cellular_component	extracellular region
C	0005768	cellular_component	endosome
C	0005771	cellular_component	multivesicular body
C	0005794	cellular_component	Golgi apparatus
C	0005886	cellular_component	plasma membrane
C	0007166	biological_process	cell surface receptor signaling pathway
C	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
C	0007399	biological_process	nervous system development
C	0008584	biological_process	male gonad development
C	0009897	cellular_component	external side of plasma membrane
C	0016167	molecular_function	glial cell-derived neurotrophic factor receptor activity
C	0016477	biological_process	cell migration
C	0019898	cellular_component	extrinsic component of membrane
C	0030182	biological_process	neuron differentiation
C	0030424	cellular_component	axon
C	0031175	biological_process	neuron projection development
C	0035860	biological_process	glial cell-derived neurotrophic factor receptor signaling pathway
C	0038023	molecular_function	signaling receptor activity
C	0038179	biological_process	neurotrophin signaling pathway
C	0043025	cellular_component	neuronal cell body
C	0043235	cellular_component	signaling receptor complex
C	0070062	cellular_component	extracellular exosome
C	0098797	cellular_component	plasma membrane protein complex
D	0001822	biological_process	kidney development
D	0005030	molecular_function	neurotrophin receptor activity
D	0005102	molecular_function	signaling receptor binding
D	0005178	molecular_function	integrin binding
D	0005576	cellular_component	extracellular region
D	0005768	cellular_component	endosome
D	0005771	cellular_component	multivesicular body
D	0005794	cellular_component	Golgi apparatus
D	0005886	cellular_component	plasma membrane
D	0007166	biological_process	cell surface receptor signaling pathway
D	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
D	0007399	biological_process	nervous system development
D	0008584	biological_process	male gonad development
D	0009897	cellular_component	external side of plasma membrane
D	0016167	molecular_function	glial cell-derived neurotrophic factor receptor activity
D	0016477	biological_process	cell migration
D	0019898	cellular_component	extrinsic component of membrane
D	0030182	biological_process	neuron differentiation
D	0030424	cellular_component	axon
D	0031175	biological_process	neuron projection development
D	0035860	biological_process	glial cell-derived neurotrophic factor receptor signaling pathway
D	0038023	molecular_function	signaling receptor activity
D	0038179	biological_process	neurotrophin signaling pathway
D	0043025	cellular_component	neuronal cell body
D	0043235	cellular_component	signaling receptor complex
D	0070062	cellular_component	extracellular exosome
D	0098797	cellular_component	plasma membrane protein complex
E	0005509	molecular_function	calcium ion binding
E	0007156	biological_process	homophilic cell-cell adhesion
E	0016020	cellular_component	membrane
F	0005509	molecular_function	calcium ion binding
F	0007156	biological_process	homophilic cell-cell adhesion
F	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CA E 2001

Chain	Residue
E	ASP266
E	SER268
E	ASP300
E	ASP302
E	ASP378

site_id	AC2
Number of Residues	6
Details	binding site for residue CA E 2002

Chain	Residue
E	ASP267
E	CA2003
E	GLU178
E	GLU232
E	ASP264
E	GLU265

site_id	AC3
Number of Residues	7
Details	binding site for residue CA E 2003

Chain	Residue
E	GLU178
E	ASN179
E	ASP230
E	GLU232
E	ASP264
E	ASP267
E	CA2002

site_id	AC4
Number of Residues	6
Details	binding site for residue CA E 2004

Chain	Residue
E	THR564
E	CYS565
E	ASP567
E	HIS569
E	GLU574
E	ASP584

site_id	AC5
Number of Residues	5
Details	binding site for residue CA F 2001

Chain	Residue
F	ASP266
F	SER268
F	ASP300
F	ASP302
F	ASP378

site_id	AC6
Number of Residues	6
Details	binding site for residue CA F 2002

Chain	Residue
F	GLU178
F	GLU232
F	ASP264
F	GLU265
F	ASP267
F	CA2003

site_id	AC7
Number of Residues	7
Details	binding site for residue CA F 2003

Chain	Residue
F	GLU178
F	ASN179
F	ASP230
F	GLU232
F	ASP264
F	ASP267
F	CA2002

site_id	AC8
Number of Residues	6
Details	binding site for residue CA F 2004

Chain	Residue
F	THR564
F	CYS565
F	ASP567
F	HIS569
F	GLU574
F	ASP584

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19478429","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25242331","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	176
Details	Repeat: {"description":"2"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	206
Details	Repeat: {"description":"3"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	228
Details	Region: {"description":"Cadherin-like region 3 (CLD3)","evidences":[{"source":"PubMed","id":"11445581","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"31535977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25242331","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4UX8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q2J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"31535977","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6Q2J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Site: {"description":"Breakpoint for translocation to form the TRIM27/RET oncogene","evidences":[{"source":"PubMed","id":"3037315","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20473317","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)