5HHW
Crystal structure of insulin receptor kinase domain in complex with cis-(R)-7-(3-(azetidin-1-ylmethyl)cyclobutyl)-5-(3-((tetrahydro-2H-pyran-2-yl)methoxy)phenyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue 60O A 1401 |
| Chain | Residue |
| A | LEU1029 |
| A | MET1103 |
| A | GLU1104 |
| A | MET1106 |
| A | ASP1110 |
| A | ARG1163 |
| A | MET1166 |
| A | ASP1177 |
| A | HOH1664 |
| A | GLY1030 |
| A | GLN1031 |
| A | SER1033 |
| A | PHE1034 |
| A | ALA1055 |
| A | LYS1057 |
| A | MET1078 |
| A | VAL1087 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 1402 |
| Chain | Residue |
| A | ARG1020 |
| A | ILE1023 |
| A | LEU1025 |
| A | PRO1129 |
| A | PRO1130 |
| A | HOH1634 |
| A | HOH1670 |
| A | HOH1694 |
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 | LEU1029-LYS1057 |
| site_id | PS00239 |
| Number of Residues | 9 |
| Details | RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR |
| Chain | Residue | Details |
| A | ASP1183-ARG1191 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 275 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9312016","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18278056","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"38056462","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14690593","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16246733","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16271887","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18278056","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18767165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26584640","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3166375","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9312016","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"14690593","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16246733","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16271887","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18278056","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18767165","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3166375","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9312016","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"27577745","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 246 |
| Chain | Residue | Details |
| A | ASN1159 | increase nucleophilicity, proton acceptor, proton donor, steric role |
| A | ARG1163 | electrostatic stabiliser, increase electrophilicity, promote heterolysis |
| A | ASN1164 | metal ligand |
| A | ASP1177 | metal ligand |
