8XJS
Cryo-EM structure of human insulin receptor bound to 3 IGF-I
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 |
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 |
B | LEU1017-LYS1045 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV |
Chain | Residue | Details |
B | PHE1143-VAL1155 |
site_id | PS00239 |
Number of Residues | 9 |
Details | RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR |
Chain | Residue | Details |
B | ASP1171-ARG1179 |
site_id | PS00262 |
Number of Residues | 15 |
Details | INSULIN Insulin family signature. CCFRsCDlrrLemyC |
Chain | Residue | Details |
D | CYS47-CYS61 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1846 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
B | HIS28-VAL758 | |
B | PRO763-PHE956 | |
A | HIS28-VAL758 | |
A | PRO763-PHE956 |
site_id | SWS_FT_FI2 |
Number of Residues | 44 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
B | SER957-LEU979 | |
A | SER957-LEU979 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9312016 |
Chain | Residue | Details |
B | PHE1159 | |
A | PHE1159 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 |
Chain | Residue | Details |
B | ILE1033 | |
A | TYR1177 | |
B | ILE1057 | |
B | ARG1104 | |
B | ILE1163 | |
B | TYR1177 | |
A | ILE1033 | |
A | ILE1057 | |
A | ARG1104 | |
A | ILE1163 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Insulin-binding => ECO:0000305 |
Chain | Residue | Details |
B | PHE66 | |
A | PHE66 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
B | SER400 | |
B | SER407 | |
A | SER400 | |
A | SER407 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
B | TYR401 | |
A | TYR401 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305 |
Chain | Residue | Details |
B | ASP992 | |
B | ILE1011 | |
A | ASP992 | |
A | ILE1011 |
site_id | SWS_FT_FI9 |
Number of Residues | 6 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:3166375 |
Chain | Residue | Details |
B | TYR999 | |
B | GLY1355 | |
B | ILE1361 | |
A | TYR999 | |
A | GLY1355 | |
A | ILE1361 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:38056462 |
Chain | Residue | Details |
B | LYS1083 | |
A | LYS1083 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
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:26584640, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016 |
Chain | Residue | Details |
B | LEU1185 | |
B | TRP1190 | |
A | LEU1185 | |
A | TRP1190 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
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 |
B | ARG1189 | |
A | ARG1189 |
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 |
B | ASN43 | |
A | ASN43 |
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 |
B | ASN52 | |
B | ASN138 | |
B | ASN282 | |
A | ASN52 | |
A | ASN138 | |
A | ASN282 |
site_id | SWS_FT_FI15 |
Number of Residues | 14 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN105 | |
A | ASN633 | |
A | ASN651 | |
A | ASN698 | |
A | GLU782 | |
A | THR933 | |
B | ASN322 | |
B | ASN633 | |
B | ASN651 | |
B | ASN698 | |
B | GLU782 | |
B | THR933 | |
A | ASN105 | |
A | ASN322 |
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 |
B | ASN242 | |
A | ASN242 |
site_id | SWS_FT_FI17 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16894147 |
Chain | Residue | Details |
B | ASN364 | |
B | ASN424 | |
A | ASN364 | |
A | ASN424 |
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 |
B | ASN445 | |
A | ASN445 |
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 |
B | ASN541 | |
A | ASN541 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2983222 |
Chain | Residue | Details |
B | PRO769 | |
A | PRO769 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 |
Chain | Residue | Details |
B | GLY920 | |
A | GLY920 |
site_id | SWS_FT_FI22 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27577745 |
Chain | Residue | Details |
B | GLY1079 | |
A | GLY1079 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 246 |
Chain | Residue | Details |
B | PHE1159 | increase nucleophilicity, proton acceptor, proton donor, steric role |
B | ILE1163 | electrostatic stabiliser, increase electrophilicity, promote heterolysis |
B | GLY1164 | metal ligand |
B | TYR1177 | metal ligand |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 246 |
Chain | Residue | Details |
A | PHE1159 | increase nucleophilicity, proton acceptor, proton donor, steric role |
A | ILE1163 | electrostatic stabiliser, increase electrophilicity, promote heterolysis |
A | GLY1164 | metal ligand |
A | TYR1177 | metal ligand |