Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6Q2N

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

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
C0001822biological_processkidney development
C0005030molecular_functionneurotrophin receptor activity
C0005102molecular_functionsignaling receptor binding
C0005178molecular_functionintegrin binding
C0005615cellular_componentextracellular space
C0005768cellular_componentendosome
C0005771cellular_componentmultivesicular body
C0005794cellular_componentGolgi apparatus
C0005886cellular_componentplasma membrane
C0007166biological_processcell surface receptor signaling pathway
C0007399biological_processnervous system development
C0008584biological_processmale gonad development
C0009897cellular_componentexternal side of plasma membrane
C0016167molecular_functionglial cell-derived neurotrophic factor receptor activity
C0016477biological_processcell migration
C0019898cellular_componentextrinsic component of membrane
C0030182biological_processneuron differentiation
C0030424cellular_componentaxon
C0031175biological_processneuron projection development
C0035860biological_processglial cell-derived neurotrophic factor receptor signaling pathway
C0038023molecular_functionsignaling receptor activity
C0038179biological_processneurotrophin signaling pathway
C0043025cellular_componentneuronal cell body
C0043235cellular_componentreceptor complex
C0050731biological_processpositive regulation of peptidyl-tyrosine phosphorylation
C0070062cellular_componentextracellular exosome
C0098552cellular_componentside of membrane
C0098797cellular_componentplasma membrane protein complex
D0001822biological_processkidney development
D0005030molecular_functionneurotrophin receptor activity
D0005102molecular_functionsignaling receptor binding
D0005178molecular_functionintegrin binding
D0005615cellular_componentextracellular space
D0005768cellular_componentendosome
D0005771cellular_componentmultivesicular body
D0005794cellular_componentGolgi apparatus
D0005886cellular_componentplasma membrane
D0007166biological_processcell surface receptor signaling pathway
D0007399biological_processnervous system development
D0008584biological_processmale gonad development
D0009897cellular_componentexternal side of plasma membrane
D0016167molecular_functionglial cell-derived neurotrophic factor receptor activity
D0016477biological_processcell migration
D0019898cellular_componentextrinsic component of membrane
D0030182biological_processneuron differentiation
D0030424cellular_componentaxon
D0031175biological_processneuron projection development
D0035860biological_processglial cell-derived neurotrophic factor receptor signaling pathway
D0038023molecular_functionsignaling receptor activity
D0038179biological_processneurotrophin signaling pathway
D0043025cellular_componentneuronal cell body
D0043235cellular_componentreceptor complex
D0050731biological_processpositive regulation of peptidyl-tyrosine phosphorylation
D0070062cellular_componentextracellular exosome
D0098552cellular_componentside of membrane
D0098797cellular_componentplasma membrane protein complex
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 PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA E 2001
ChainResidue
EASP266
ESER268
EASP300
EASP302
EASP378

site_idAC2
Number of Residues6
Detailsbinding site for residue CA E 2002
ChainResidue
EASP267
ECA2003
EGLU178
EGLU232
EASP264
EGLU265

site_idAC3
Number of Residues7
Detailsbinding site for residue CA E 2003
ChainResidue
EGLU178
EASN179
EASP230
EGLU232
EASP264
EASP267
ECA2002

site_idAC4
Number of Residues6
Detailsbinding site for residue CA E 2004
ChainResidue
ETHR564
ECYS565
EASP567
EHIS569
EGLU574
EASP584

site_idAC5
Number of Residues5
Detailsbinding site for residue CA F 2001
ChainResidue
FASP266
FSER268
FASP300
FASP302
FASP378

site_idAC6
Number of Residues6
Detailsbinding site for residue CA F 2002
ChainResidue
FGLU178
FGLU232
FASP264
FGLU265
FASP267
FCA2003

site_idAC7
Number of Residues7
Detailsbinding site for residue CA F 2003
ChainResidue
FGLU178
FASN179
FASP230
FGLU232
FASP264
FASP267
FCA2002

site_idAC8
Number of Residues6
Detailsbinding site for residue CA F 2004
ChainResidue
FTHR564
FCYS565
FASP567
FHIS569
FGLU574
FASP584

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1212
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ELEU29-ARG635
FLEU29-ARG635
CASN406
DASN59
DASN347
DASN406

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:31535977, ECO:0000305|PubMed:25242331, ECO:0007744|PDB:4UX8, ECO:0007744|PDB:6Q2J
ChainResidueDetails
EGLU178
FASP230
FASP264
FGLU265
FASP266
FSER268
FASP300
FASP302
EASP230
EASP264
EGLU265
EASP266
ESER268
EASP300
EASP302
FGLU178

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:31535977, ECO:0007744|PDB:6Q2J
ChainResidueDetails
EASN179
EASP584
FASN179
FGLU232
FASP267
FASP378
FTHR564
FCYS565
FASP567
FHIS569
FGLU574
EGLU232
FASP584
EASP267
EASP378
ETHR564
ECYS565
EASP567
EHIS569
EGLU574

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Breakpoint for translocation to form the TRIM27/RET oncogene => ECO:0000269|PubMed:3037315
ChainResidueDetails
EARG587
FARG587

site_idSWS_FT_FI5
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_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20473317
ChainResidueDetails
EASN151
FASN151

224004

PDB entries from 2024-08-21

PDB statisticsPDBj update infoContact PDBjnumon