8U4C
Cryo-EM structure of long form insulin receptor (IR-B) with four IGF2 bound, symmetric conformation.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
| A | 0016020 | cellular_component | membrane |
| A | 0043548 | molecular_function | phosphatidylinositol 3-kinase binding |
| A | 0043560 | molecular_function | insulin receptor substrate binding |
| A | 0046777 | biological_process | protein autophosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
| B | 0016020 | cellular_component | membrane |
| B | 0043548 | molecular_function | phosphatidylinositol 3-kinase binding |
| B | 0043560 | molecular_function | insulin receptor substrate binding |
| B | 0046777 | biological_process | protein autophosphorylation |
| C | 0005179 | molecular_function | hormone activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0008083 | molecular_function | growth factor activity |
| D | 0005179 | molecular_function | hormone activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005615 | cellular_component | extracellular space |
| D | 0008083 | molecular_function | growth factor activity |
| E | 0005179 | molecular_function | hormone activity |
| E | 0005576 | cellular_component | extracellular region |
| E | 0005615 | cellular_component | extracellular space |
| E | 0008083 | molecular_function | growth factor activity |
| F | 0005179 | molecular_function | hormone activity |
| F | 0005576 | cellular_component | extracellular region |
| F | 0005615 | cellular_component | extracellular space |
| F | 0008083 | molecular_function | growth factor activity |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 29 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnardiikgeaetr.....VAVK |
| Chain | Residue | Details |
| A | LEU1002-LYS1030 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV |
| Chain | Residue | Details |
| A | PHE1128-VAL1140 |
| site_id | PS00239 |
| Number of Residues | 9 |
| Details | RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR |
| Chain | Residue | Details |
| A | ASP1156-ARG1164 |
| site_id | PS00262 |
| Number of Residues | 15 |
| Details | INSULIN Insulin family signature. CCFRsCDlalLetyC |
| Chain | Residue | Details |
| C | CYS46-CYS60 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | SITE: Important for interaction with integrin => ECO:0000269|PubMed:28873464 |
| Chain | Residue | Details |
| C | ARG24 | |
| E | ARG34 | |
| E | ARG37 | |
| E | ARG38 | |
| F | ARG24 | |
| F | ARG34 | |
| F | ARG37 | |
| F | ARG38 | |
| C | ARG34 | |
| C | ARG37 | |
| C | ARG38 | |
| D | ARG24 | |
| D | ARG34 | |
| D | ARG37 | |
| D | ARG38 | |
| E | ARG24 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360 |
| Chain | Residue | Details |
| C | THR72 | |
| D | THR72 | |
| E | THR72 | |
| F | THR72 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:1569071, ECO:0000269|PubMed:22171320 |
| Chain | Residue | Details |
| C | THR75 | |
| D | THR75 | |
| E | THR75 | |
| F | THR75 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320 |
| Chain | Residue | Details |
| C | THR139 | |
| D | THR139 | |
| E | THR139 | |
| F | THR139 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 |
| Chain | Residue | Details |
| A | SER1006 | |
| B | ASP1150 | |
| A | LYS1030 | |
| A | GLU1077 | |
| A | ARG1136 | |
| A | ASP1150 | |
| B | SER1006 | |
| B | LYS1030 | |
| B | GLU1077 | |
| B | ARG1136 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Insulin-binding => ECO:0000305 |
| Chain | Residue | Details |
| A | PHE39 | |
| B | PHE39 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | SER373 | |
| A | SER380 | |
| B | SER373 | |
| B | SER380 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | TYR374 | |
| B | TYR374 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305 |
| Chain | Residue | Details |
| A | TYR965 | |
| A | TYR984 | |
| B | TYR965 | |
| B | TYR984 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:3166375 |
| Chain | Residue | Details |
| A | TYR972 | |
| A | TYR1328 | |
| A | TYR1334 | |
| B | TYR972 | |
| B | TYR1328 | |
| B | TYR1334 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:38056462 |
| Chain | Residue | Details |
| A | CYS1056 | |
| B | CYS1056 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 6 |
| Details | MOD_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 |
| Chain | Residue | Details |
| A | TYR1158 | |
| A | TYR1162 | |
| A | TYR1163 | |
| B | TYR1158 | |
| B | TYR1162 | |
| B | TYR1163 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:23302862, ECO:0000269|PubMed:2983222 |
| Chain | Residue | Details |
| A | ASN16 | |
| B | ASN16 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:23302862 |
| Chain | Residue | Details |
| A | ASN25 | |
| A | ASN111 | |
| A | ASN255 | |
| B | ASN25 | |
| B | ASN111 | |
| B | ASN255 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 14 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN78 | |
| B | ASN606 | |
| B | ASN624 | |
| B | ASN671 | |
| B | ASN755 | |
| B | ASN906 | |
| A | ASN295 | |
| A | ASN606 | |
| A | ASN624 | |
| A | ASN671 | |
| A | ASN755 | |
| A | ASN906 | |
| B | ASN78 | |
| B | ASN295 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23302862 |
| Chain | Residue | Details |
| A | ASN215 | |
| B | ASN215 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147 |
| Chain | Residue | Details |
| A | ASN337 | |
| A | ASN397 | |
| B | ASN337 | |
| B | ASN397 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147, ECO:0000269|PubMed:19349973 |
| Chain | Residue | Details |
| A | ASN418 | |
| B | ASN418 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1472036, ECO:0000269|PubMed:19159218 |
| Chain | Residue | Details |
| A | ASN514 | |
| B | ASN514 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2983222 |
| Chain | Residue | Details |
| A | ASN742 | |
| B | ASN742 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 |
| Chain | Residue | Details |
| A | ASN893 | |
| B | ASN893 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 246 |
| Chain | Residue | Details |
| A | ASP1132 | increase nucleophilicity, proton acceptor, proton donor, steric role |
| A | ARG1136 | electrostatic stabiliser, increase electrophilicity, promote heterolysis |
| A | ASN1137 | metal ligand |
| A | ASP1150 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 246 |
| Chain | Residue | Details |
| B | ASP1132 | increase nucleophilicity, proton acceptor, proton donor, steric role |
| B | ARG1136 | electrostatic stabiliser, increase electrophilicity, promote heterolysis |
| B | ASN1137 | metal ligand |
| B | ASP1150 | metal ligand |
