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8EYR

Cryo-EM structure of two IGF1 bound full-length mouse IGF1R mutant (four glycine residues inserted in the alpha-CT; IGF1R-P674G4): symmetric conformation

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
A0016020cellular_componentmembrane
A0043548molecular_functionphosphatidylinositol 3-kinase binding
A0043560molecular_functioninsulin receptor substrate binding
A0046777biological_processprotein autophosphorylation
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
B0016020cellular_componentmembrane
B0043548molecular_functionphosphatidylinositol 3-kinase binding
B0043560molecular_functioninsulin receptor substrate binding
B0046777biological_processprotein autophosphorylation
C0005179molecular_functionhormone activity
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0008083molecular_functiongrowth factor activity
D0005179molecular_functionhormone activity
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0008083molecular_functiongrowth factor activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGvakgvvkdepetr.....VAIK
ChainResidueDetails
BLEU980-LYS1008

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV
ChainResidueDetails
BPHE1107-VAL1119

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR
ChainResidueDetails
BASP1135-ARG1143

site_idPS00262
Number of Residues15
DetailsINSULIN Insulin family signature. CCFRsCDlrrLemyC
ChainResidueDetails
CCYS47-CYS61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues388
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BASP716-HIS910
AASP716-HIS910

site_idSWS_FT_FI2
Number of Residues46
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BLEU911-HIS934
ALEU911-HIS934

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
BASP1111
AASP1111

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU980
BLYS1008
ALEU980
ALYS1008

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P08069
ChainResidueDetails
BTYR955
ATYR955

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:P08069
ChainResidueDetails
BTYR1137
BTYR1141
BTYR1142
ATYR1137
ATYR1141
ATYR1142

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by GSK3-beta => ECO:0000269|PubMed:22685298
ChainResidueDetails
BSER1254
ASER1254

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:22685298
ChainResidueDetails
BSER1258
ASER1258

site_idSWS_FT_FI9
Number of Residues22
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN21
BASN593
BASN888
AASN21
AASN72
AASN105
AASN215
AASN284
AASN388
AASN409
AASN505
BASN72
AASN578
AASN593
AASN888
BASN105
BASN215
BASN284
BASN388
BASN409
BASN505
BASN578

site_idSWS_FT_FI10
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
BASN611
BASN731
BASN739
AASN611
AASN731
AASN739

site_idSWS_FT_FI11
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19656770
ChainResidueDetails
BASN722
BASN875
AASN722
AASN875

site_idSWS_FT_FI12
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P08069
ChainResidueDetails
BLYS1144
BLYS1147
ALYS1144
ALYS1147

227344

PDB entries from 2024-11-13

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