7STI
Full-length insulin receptor bound with unsaturated insulin WT (1 insulin bound) asymmetric 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 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 29 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnakdiikgeaetr.....VAVK |
Chain | Residue | Details |
A | LEU990-LYS1018 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV |
Chain | Residue | Details |
A | PHE1116-VAL1128 |
site_id | PS00239 |
Number of Residues | 9 |
Details | RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR |
Chain | Residue | Details |
A | ASP1144-ARG1152 |
site_id | PS00262 |
Number of Residues | 15 |
Details | INSULIN Insulin family signature. CCTSiCSlyqLenyC |
Chain | Residue | Details |
C | CYS61-CYS75 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1826 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
A | HIS1-SER719 | |
A | SER724-LYS917 | |
B | HIS1-SER719 | |
B | SER724-LYS917 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | ILE918-LEU938 | |
B | ILE918-LEU938 |
site_id | SWS_FT_FI3 |
Number of Residues | 808 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
A | PHE939-SER1343 | |
B | PHE939-SER1343 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250 |
Chain | Residue | Details |
A | ASP1120 | |
B | ASP1120 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | SER994 | |
A | GLU1065 | |
A | ARG1124 | |
A | ASP1138 | |
B | SER994 | |
B | GLU1065 | |
B | ARG1124 | |
B | ASP1138 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS1018 | |
B | LYS1018 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Insulin-binding => ECO:0000250 |
Chain | Residue | Details |
A | PHE39 | |
B | PHE39 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06213 |
Chain | Residue | Details |
A | SER373 | |
A | SER380 | |
B | SER373 | |
B | SER380 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06213 |
Chain | Residue | Details |
A | TYR374 | |
B | TYR374 |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:P06213 |
Chain | Residue | Details |
A | TYR960 | |
A | TYR1146 | |
A | TYR1316 | |
A | TYR1322 | |
B | TYR960 | |
B | TYR1146 | |
B | TYR1316 | |
B | TYR1322 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P06213 |
Chain | Residue | Details |
A | CYS1044 | |
B | CYS1044 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20655470 |
Chain | Residue | Details |
A | TYR1150 | |
A | TYR1151 | |
B | TYR1150 | |
B | TYR1151 |
site_id | SWS_FT_FI13 |
Number of Residues | 34 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN16 | |
A | ASN514 | |
A | ASN606 | |
A | ASN624 | |
A | ASN671 | |
A | ASN730 | |
A | ASN743 | |
A | ASN881 | |
A | ASN894 | |
B | ASN16 | |
B | ASN25 | |
A | ASN25 | |
B | ASN78 | |
B | ASN111 | |
B | ASN215 | |
B | ASN255 | |
B | ASN295 | |
B | ASN337 | |
B | ASN397 | |
B | ASN514 | |
B | ASN606 | |
B | ASN624 | |
A | ASN78 | |
B | ASN671 | |
B | ASN730 | |
B | ASN743 | |
B | ASN881 | |
B | ASN894 | |
A | ASN111 | |
A | ASN215 | |
A | ASN255 | |
A | ASN295 | |
A | ASN337 | |
A | ASN397 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770 |
Chain | Residue | Details |
A | ASN418 | |
B | ASN418 |