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7STK

Full-length insulin receptor bound with unsaturated insulin WT (2 insulins bound) asymmetric conformation (Conformation 2)

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
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnakdiikgeaetr.....VAVK
ChainResidueDetails
ALEU990-LYS1018

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV
ChainResidueDetails
APHE1116-VAL1128

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR
ChainResidueDetails
AASP1144-ARG1152

site_idPS00262
Number of Residues15
DetailsINSULIN Insulin family signature. CCTSiCSlyqLenyC
ChainResidueDetails
CCYS61-CYS75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1826
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AHIS1-SER719
ASER724-LYS917
BHIS1-SER719
BSER724-LYS917

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AILE918-LEU938
BILE918-LEU938

site_idSWS_FT_FI3
Number of Residues808
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
APHE939-SER1343
BPHE939-SER1343

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250
ChainResidueDetails
AASP1120
BASP1120

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ASER994
AGLU1065
AARG1124
AASP1138
BSER994
BGLU1065
BARG1124
BASP1138

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS1018
BLYS1018

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
ATYR960
ATYR1146
ATYR1316
ATYR1322
BTYR960
BTYR1146
BTYR1316
BTYR1322

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20655470
ChainResidueDetails
ATYR1150
ATYR1151
BTYR1150
BTYR1151

site_idSWS_FT_FI12
Number of Residues34
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN16
AASN514
AASN606
AASN624
AASN671
AASN730
AASN743
AASN881
AASN894
BASN16
BASN25
AASN25
BASN78
BASN111
BASN215
BASN255
BASN295
BASN337
BASN397
BASN514
BASN606
BASN624
AASN78
BASN671
BASN730
BASN743
BASN881
BASN894
AASN111
AASN215
AASN255
AASN295
AASN337
AASN397

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770
ChainResidueDetails
AASN418
BASN418

218853

PDB entries from 2024-04-24

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