7TYJ
Cryo-EM Structure of insulin receptor-related receptor (IRR) in apo-state captured at pH 7. The 3D refinement was focused on one of two halves with C1 symmetry applied
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 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 29 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGlargleageestp.....VALK |
Chain | Residue | Details |
A | LEU959-LYS987 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV |
Chain | Residue | Details |
A | PHE1085-VAL1097 |
site_id | PS00239 |
Number of Residues | 9 |
Details | RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DVYetdYYR |
Chain | Residue | Details |
A | ASP1113-ARG1121 |
site_id | PS00430 |
Number of Residues | 32 |
Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mavpslwpwgaclpviflslgfgl...........................................................................................DTVEVCPS |
Chain | Residue | Details |
A | MET-25-SER6 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 348 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | ALA721-HIS895 | |
B | ALA721-HIS895 |
site_id | SWS_FT_FI2 |
Number of Residues | 42 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | VAL896-PHE917 | |
B | VAL896-PHE917 |
site_id | SWS_FT_FI3 |
Number of Residues | 706 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | TYR918-HIS1271 | |
B | TYR918-HIS1271 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
Chain | Residue | Details |
A | ASP1089 | |
B | ASP1089 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU959 | |
A | LYS987 | |
B | LEU959 | |
B | LYS987 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305 |
Chain | Residue | Details |
A | TYR1119 | |
A | TYR1120 | |
B | TYR1119 | |
B | TYR1120 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN21 | |
A | ASN872 | |
B | ASN21 | |
B | ASN285 | |
B | ASN385 | |
B | ASN466 | |
B | ASN502 | |
B | ASN590 | |
B | ASN608 | |
B | ASN730 | |
B | ASN859 | |
A | ASN285 | |
B | ASN872 | |
A | ASN385 | |
A | ASN466 | |
A | ASN502 | |
A | ASN590 | |
A | ASN608 | |
A | ASN730 | |
A | ASN859 |