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6Q2R

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0008083molecular_functiongrowth factor activity
A0030116molecular_functionglial cell-derived neurotrophic factor receptor binding
A0030971molecular_functionreceptor tyrosine kinase binding
B0008083molecular_functiongrowth factor activity
B0030116molecular_functionglial cell-derived neurotrophic factor receptor binding
B0030971molecular_functionreceptor tyrosine kinase binding
C0038023molecular_functionsignaling receptor activity
D0038023molecular_functionsignaling receptor activity
E0005509molecular_functioncalcium ion binding
E0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
E0016020cellular_componentmembrane
F0005509molecular_functioncalcium ion binding
F0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
F0016020cellular_componentmembrane
U0008083molecular_functiongrowth factor activity
U0030116molecular_functionglial cell-derived neurotrophic factor receptor binding
U0030971molecular_functionreceptor tyrosine kinase binding
V0008083molecular_functiongrowth factor activity
V0030116molecular_functionglial cell-derived neurotrophic factor receptor binding
V0030971molecular_functionreceptor tyrosine kinase binding
W0038023molecular_functionsignaling receptor activity
X0038023molecular_functionsignaling receptor activity
Y0005509molecular_functioncalcium ion binding
Y0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
Y0016020cellular_componentmembrane
Z0005509molecular_functioncalcium ion binding
Z0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
Z0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29414779","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues52
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues456
DetailsRegion: {"description":"Cadherin-like region 3 (CLD3)","evidences":[{"source":"PubMed","id":"11445581","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues404
DetailsRegion: {"description":"Cadherin-like region 4 (CLD4)","evidences":[{"source":"PubMed","id":"11445581","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues32
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31535977","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6Q2J","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsSite: {"description":"Breakpoint for translocation to form the TRIM27/RET oncogene","evidences":[{"source":"PubMed","id":"3037315","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20473317","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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