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6Q2J

Cryo-EM structure of extracellular dimeric complex of RET/GFRAL/GDF15

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008083molecular_functiongrowth factor activity
B0005576cellular_componentextracellular region
B0008083molecular_functiongrowth factor activity
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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1212
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ELEU29-ARG635
DASN67
DASN103
DASN116
FLEU29-ARG635
CASN62
CASN67
CASN103
CASN116
DASN23
DASN50
DASN62

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Breakpoint for translocation to form the TRIM27/RET oncogene
ChainResidueDetails
EARG587
FARG587

site_idSWS_FT_FI3
Number of Residues22
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
EASN98
EASN468
EASN554
FASN98
FASN199
FASN336
FASN343
FASN361
FASN367
FASN377
FASN394
EASN199
FASN448
FASN468
FASN554
EASN336
EASN343
EASN361
EASN367
EASN377
EASN394
EASN448

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20473317
ChainResidueDetails
EASN151
FASN151

218853

PDB entries from 2024-04-24

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