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8DFP

Ectodomain of full-length KIT(DupA502,Y503)-SCF dimers

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
A0019955molecular_functioncytokine binding
A0038093biological_processFc receptor signaling pathway
A0038109biological_processKit signaling pathway
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
B0019955molecular_functioncytokine binding
B0038093biological_processFc receptor signaling pathway
B0038109biological_processKit signaling pathway
C0005173molecular_functionstem cell factor receptor binding
C0007155biological_processcell adhesion
C0016020cellular_componentmembrane
D0005173molecular_functionstem cell factor receptor binding
D0007155biological_processcell adhesion
D0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNILL
ChainResidueDetails
ACYS786-LEU798

site_idPS00240
Number of Residues14
DetailsRECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GnHmNIVNLLGACT
ChainResidueDetails
AGLY646-THR659

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues168
DetailsDomain: {"description":"Ig-like C2-type 2"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues192
DetailsDomain: {"description":"Ig-like C2-type 3"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues186
DetailsDomain: {"description":"Ig-like C2-type 4"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17662946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17662946","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Not glycosylated"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","evidences":[{"source":"PubMed","id":"1381905","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1381905","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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