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8XJS

Cryo-EM structure of human insulin receptor bound to 3 IGF-I

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
E0005179molecular_functionhormone activity
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0008083molecular_functiongrowth factor activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnardiikgeaetr.....VAVK
ChainResidueDetails
BLEU1017-LYS1045

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV
ChainResidueDetails
BPHE1143-VAL1155

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR
ChainResidueDetails
BASP1171-ARG1179

site_idPS00262
Number of Residues15
DetailsINSULIN Insulin family signature. CCFRsCDlrrLemyC
ChainResidueDetails
DCYS47-CYS61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1846
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
BHIS28-VAL758
BPRO763-PHE956
AHIS28-VAL758
APRO763-PHE956

site_idSWS_FT_FI2
Number of Residues44
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BSER957-LEU979
ASER957-LEU979

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9312016
ChainResidueDetails
BPHE1159
APHE1159

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056
ChainResidueDetails
BILE1033
ATYR1177
BILE1057
BARG1104
BILE1163
BTYR1177
AILE1033
AILE1057
AARG1104
AILE1163

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Insulin-binding => ECO:0000305
ChainResidueDetails
BPHE66
APHE66

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
BSER400
BSER407
ASER400
ASER407

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648
ChainResidueDetails
BTYR401
ATYR401

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305
ChainResidueDetails
BASP992
BILE1011
AASP992
AILE1011

site_idSWS_FT_FI9
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:3166375
ChainResidueDetails
BTYR999
BGLY1355
BILE1361
ATYR999
AGLY1355
AILE1361

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:38056462
ChainResidueDetails
BLYS1083
ALYS1083

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:26584640, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016
ChainResidueDetails
BLEU1185
BTRP1190
ALEU1185
ATRP1190

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016
ChainResidueDetails
BARG1189
AARG1189

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:23302862, ECO:0000269|PubMed:2983222
ChainResidueDetails
BASN43
AASN43

site_idSWS_FT_FI14
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:23302862
ChainResidueDetails
BASN52
BASN138
BASN282
AASN52
AASN138
AASN282

site_idSWS_FT_FI15
Number of Residues14
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN105
AASN633
AASN651
AASN698
AGLU782
ATHR933
BASN322
BASN633
BASN651
BASN698
BGLU782
BTHR933
AASN105
AASN322

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23302862
ChainResidueDetails
BASN242
AASN242

site_idSWS_FT_FI17
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147
ChainResidueDetails
BASN364
BASN424
AASN364
AASN424

site_idSWS_FT_FI18
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19349973
ChainResidueDetails
BASN445
AASN445

site_idSWS_FT_FI19
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1472036, ECO:0000269|PubMed:19159218
ChainResidueDetails
BASN541
AASN541

site_idSWS_FT_FI20
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2983222
ChainResidueDetails
BPRO769
APRO769

site_idSWS_FT_FI21
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
BGLY920
AGLY920

site_idSWS_FT_FI22
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27577745
ChainResidueDetails
BGLY1079
AGLY1079

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 246
ChainResidueDetails
BPHE1159increase nucleophilicity, proton acceptor, proton donor, steric role
BILE1163electrostatic stabiliser, increase electrophilicity, promote heterolysis
BGLY1164metal ligand
BTYR1177metal ligand

site_idMCSA2
Number of Residues4
DetailsM-CSA 246
ChainResidueDetails
APHE1159increase nucleophilicity, proton acceptor, proton donor, steric role
AILE1163electrostatic stabiliser, increase electrophilicity, promote heterolysis
AGLY1164metal ligand
ATYR1177metal ligand

236620

PDB entries from 2025-05-28

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