8X2M
Cryo-EM structure of the IR/IGF-I complex, conformation 2
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 | 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. CCFRsCDlrrLemyC |
| Chain | Residue | Details |
| C | 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 |
| A | HIS1-VAL731 | |
| A | PRO736-PHE929 | |
| B | HIS1-VAL731 | |
| B | PRO736-PHE929 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | SER930-LEU952 | |
| B | SER930-LEU952 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9312016 |
| Chain | Residue | Details |
| A | PHE1132 | |
| B | PHE1132 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056 |
| Chain | Residue | Details |
| A | ILE1006 | |
| B | TYR1150 | |
| A | ILE1030 | |
| A | ARG1077 | |
| A | ILE1136 | |
| A | TYR1150 | |
| B | ILE1006 | |
| B | ILE1030 | |
| B | ARG1077 | |
| B | ILE1136 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Insulin-binding => ECO:0000305 |
| Chain | Residue | Details |
| A | PHE39 | |
| B | PHE39 |
| site_id | SWS_FT_FI6 |
| 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_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | TYR374 | |
| B | TYR374 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305 |
| Chain | Residue | Details |
| A | ASP965 | |
| A | ILE984 | |
| B | ASP965 | |
| B | ILE984 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:3166375 |
| Chain | Residue | Details |
| A | TYR972 | |
| A | GLY1328 | |
| A | ILE1334 | |
| B | TYR972 | |
| B | GLY1328 | |
| B | ILE1334 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:38056462 |
| Chain | Residue | Details |
| A | LYS1056 | |
| B | LYS1056 |
| site_id | SWS_FT_FI11 |
| 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 | LEU1158 | |
| A | ARG1162 | |
| A | TRP1163 | |
| B | LEU1158 | |
| B | ARG1162 | |
| B | TRP1163 |
| site_id | SWS_FT_FI12 |
| 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_FI13 |
| 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_FI14 |
| Number of Residues | 14 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN78 | |
| B | ASN606 | |
| B | ASN624 | |
| B | ASN671 | |
| B | GLU755 | |
| B | THR906 | |
| A | ASN295 | |
| A | ASN606 | |
| A | ASN624 | |
| A | ASN671 | |
| A | GLU755 | |
| A | THR906 | |
| B | ASN78 | |
| B | ASN295 |
| site_id | SWS_FT_FI15 |
| 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_FI16 |
| 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_FI17 |
| 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_FI18 |
| 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_FI19 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2983222 |
| Chain | Residue | Details |
| A | PRO742 | |
| B | PRO742 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 |
| Chain | Residue | Details |
| A | GLY893 | |
| B | GLY893 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 246 |
| Chain | Residue | Details |
| A | PHE1132 | increase nucleophilicity, proton acceptor, proton donor, steric role |
| A | ILE1136 | electrostatic stabiliser, increase electrophilicity, promote heterolysis |
| A | GLY1137 | metal ligand |
| A | TYR1150 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 246 |
| Chain | Residue | Details |
| B | PHE1132 | increase nucleophilicity, proton acceptor, proton donor, steric role |
| B | ILE1136 | electrostatic stabiliser, increase electrophilicity, promote heterolysis |
| B | GLY1137 | metal ligand |
| B | TYR1150 | metal ligand |
