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7TYK

Cryo-EM Structure of insulin receptor-related receptor (IRR) in apo-state captured at pH 7. The 3D refinement was applied with C2 symmetry

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
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGlargleageestp.....VALK
ChainResidueDetails
ALEU959-LYS987

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV
ChainResidueDetails
APHE1085-VAL1097

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DVYetdYYR
ChainResidueDetails
AASP1113-ARG1121

site_idPS00430
Number of Residues32
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mavpslwpwgaclpviflslgfgl...........................................................................................DTVEVCPS
ChainResidueDetails
AMET-25-SER6

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues348
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AALA721-HIS895
BALA721-HIS895

site_idSWS_FT_FI2
Number of Residues42
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AVAL896-PHE917
BVAL896-PHE917

site_idSWS_FT_FI3
Number of Residues706
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ATYR918-HIS1271
BTYR918-HIS1271

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP1089
BASP1089

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU959
ALYS987
BLEU959
BLYS987

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305
ChainResidueDetails
ATYR1119
ATYR1120
BTYR1119
BTYR1120

site_idSWS_FT_FI7
Number of Residues20
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN21
AASN872
BASN21
BASN285
BASN385
BASN466
BASN502
BASN590
BASN608
BASN730
BASN859
AASN285
BASN872
AASN385
AASN466
AASN502
AASN590
AASN608
AASN730
AASN859

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PDB entries from 2024-11-06

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