7SL3
Full-length insulin receptor bound with site 2 binding deficient mutant insulin (A-L13R) -- 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 |
| D | 0005179 | molecular_function | hormone activity |
| D | 0005576 | cellular_component | extracellular region |
| E | 0005179 | molecular_function | hormone activity |
| E | 0005576 | cellular_component | extracellular region |
| F | 0005179 | molecular_function | hormone activity |
| F | 0005576 | cellular_component | extracellular region |
Functional Information from PROSITE/UniProt
| site_id | PS00262 |
| Number of Residues | 15 |
| Details | INSULIN Insulin family signature. CCTSiCSryqLenyC |
| Chain | Residue | Details |
| E | CYS6-CYS20 |
| site_id | PS00107 |
| Number of Residues | 29 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnakdiikgeaetr.....VAVK |
| Chain | Residue | Details |
| A | LEU992-LYS1020 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV |
| Chain | Residue | Details |
| A | PHE1118-VAL1130 |
| site_id | PS00239 |
| Number of Residues | 9 |
| Details | RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR |
| Chain | Residue | Details |
| A | ASP1146-ARG1154 |
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-SER721 | |
| A | SER726-LYS919 | |
| B | HIS1-SER721 | |
| B | SER726-LYS919 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | ILE920-LEU940 | |
| B | ILE920-LEU940 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 808 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | PHE941-SER1345 | |
| B | PHE941-SER1345 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP1122 | |
| B | ASP1122 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | SER996 | |
| A | GLU1067 | |
| A | ARG1126 | |
| A | ASP1140 | |
| B | SER996 | |
| B | GLU1067 | |
| B | ARG1126 | |
| B | ASP1140 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS1020 | |
| B | LYS1020 |
| 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 | TYR962 | |
| A | TYR1148 | |
| A | TYR1318 | |
| A | TYR1324 | |
| B | TYR962 | |
| B | TYR1148 | |
| B | TYR1318 | |
| B | TYR1324 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20655470 |
| Chain | Residue | Details |
| A | TYR1152 | |
| A | TYR1153 | |
| B | TYR1152 | |
| B | TYR1153 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 34 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN16 | |
| A | ASN514 | |
| A | ASN608 | |
| A | ASN626 | |
| A | ASN673 | |
| A | ASN732 | |
| A | ASN745 | |
| A | ASN883 | |
| A | ASN896 | |
| B | ASN16 | |
| B | ASN25 | |
| A | ASN25 | |
| B | ASN78 | |
| B | ASN111 | |
| B | ASN215 | |
| B | ASN255 | |
| B | ASN295 | |
| B | ASN337 | |
| B | ASN397 | |
| B | ASN514 | |
| B | ASN608 | |
| B | ASN626 | |
| A | ASN78 | |
| B | ASN673 | |
| B | ASN732 | |
| B | ASN745 | |
| B | ASN883 | |
| B | ASN896 | |
| A | ASN111 | |
| A | ASN215 | |
| A | ASN255 | |
| A | ASN295 | |
| A | ASN337 | |
| A | ASN397 |
| site_id | SWS_FT_FI13 |
| 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 |
