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7SL3

Full-length insulin receptor bound with site 2 binding deficient mutant insulin (A-L13R) -- 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
D0005179molecular_functionhormone activity
D0005576cellular_componentextracellular region
E0005179molecular_functionhormone activity
E0005576cellular_componentextracellular region
F0005179molecular_functionhormone activity
F0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnakdiikgeaetr.....VAVK
ChainResidueDetails
ALEU992-LYS1020

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV
ChainResidueDetails
APHE1118-VAL1130

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR
ChainResidueDetails
AASP1146-ARG1154

site_idPS00262
Number of Residues15
DetailsINSULIN Insulin family signature. CCTSiCSryqLenyC
ChainResidueDetails
ECYS6-CYS20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1826
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AHIS1-SER721
ASER726-LYS919
BHIS1-SER721
BSER726-LYS919

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AILE920-LEU940
BILE920-LEU940

site_idSWS_FT_FI3
Number of Residues808
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
APHE941-SER1345
BPHE941-SER1345

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250
ChainResidueDetails
AASP1122
BASP1122

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ASER996
AGLU1067
AARG1126
AASP1140
BSER996
BGLU1067
BARG1126
BASP1140

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS1020
BLYS1020

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Insulin-binding => ECO:0000250
ChainResidueDetails
APHE39
BPHE39

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06213
ChainResidueDetails
ASER373
ASER380
BSER373
BSER380

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06213
ChainResidueDetails
ATYR374
BTYR374

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:P06213
ChainResidueDetails
ATYR962
ATYR1148
ATYR1318
ATYR1324
BTYR962
BTYR1148
BTYR1318
BTYR1324

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P06213
ChainResidueDetails
ACYS1046
BCYS1046

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20655470
ChainResidueDetails
ATYR1152
ATYR1153
BTYR1152
BTYR1153

site_idSWS_FT_FI13
Number of Residues34
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN16
AASN514
AASN608
AASN626
AASN673
AASN732
AASN745
AASN883
AASN896
BASN16
BASN25
AASN25
BASN78
BASN111
BASN215
BASN255
BASN295
BASN337
BASN397
BASN514
BASN608
BASN626
AASN78
BASN673
BASN732
BASN745
BASN883
BASN896
AASN111
AASN215
AASN255
AASN295
AASN337
AASN397

site_idSWS_FT_FI14
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770
ChainResidueDetails
AASN418
BASN418

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PDB entries from 2024-11-13

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