2ZM3
Complex Structure of Insulin-like Growth Factor Receptor and Isoquinolinedione Inhibitor
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 |
| 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 |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
| C | 0016020 | cellular_component | membrane |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004713 | molecular_function | protein tyrosine kinase activity |
| D | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
| D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 575 A 1 |
| Chain | Residue |
| A | LEU1005 |
| A | GLN1007 |
| A | ALA1031 |
| A | MET1079 |
| A | GLU1080 |
| A | LEU1081 |
| A | MET1082 |
| A | THR1083 |
| A | MET1142 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 575 D 1 |
| Chain | Residue |
| D | LEU1005 |
| D | GLN1007 |
| D | ALA1031 |
| D | MET1079 |
| D | GLU1080 |
| D | LEU1081 |
| D | MET1082 |
| D | THR1083 |
| D | MET1142 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 575 B 1 |
| Chain | Residue |
| B | LEU1005 |
| B | ALA1031 |
| B | LYS1033 |
| B | MET1079 |
| B | GLU1080 |
| B | LEU1081 |
| B | MET1082 |
| B | THR1083 |
| B | MET1142 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 575 C 1 |
| Chain | Residue |
| C | LEU1005 |
| C | GLN1007 |
| C | ALA1031 |
| C | MET1079 |
| C | GLU1080 |
| C | LEU1081 |
| C | MET1082 |
| C | THR1083 |
| C | MET1142 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 29 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGvakgvvkdepetr.....VAIK |
| Chain | Residue | Details |
| A | LEU1005-LYS1033 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV |
| Chain | Residue | Details |
| A | PHE1131-VAL1143 |
| site_id | PS00239 |
| Number of Residues | 9 |
| Details | RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR |
| Chain | Residue | Details |
| A | ASP1159-ARG1167 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
| Chain | Residue | Details |
| A | ASP1135 | |
| B | ASP1135 | |
| C | ASP1135 | |
| D | ASP1135 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LEU1005 | |
| B | LEU1005 | |
| C | LEU1005 | |
| D | LEU1005 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS1033 | |
| B | LYS1033 | |
| C | LYS1033 | |
| D | LYS1033 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11694888, ECO:0000269|PubMed:18501599, ECO:0000269|PubMed:19041240 |
| Chain | Residue | Details |
| A | PTR1161 | |
| D | PTR1161 | |
| D | PTR1165 | |
| D | PTR1166 | |
| A | PTR1165 | |
| A | PTR1166 | |
| B | PTR1161 | |
| B | PTR1165 | |
| B | PTR1166 | |
| C | PTR1161 | |
| C | PTR1165 | |
| C | PTR1166 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by GSK3-beta => ECO:0000250|UniProtKB:Q60751 |
| Chain | Residue | Details |
| A | SER1278 | |
| B | SER1278 | |
| C | SER1278 | |
| D | SER1278 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q60751 |
| Chain | Residue | Details |
| A | SER1282 | |
| B | SER1282 | |
| C | SER1282 | |
| D | SER1282 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:21994939 |
| Chain | Residue | Details |
| A | LYS1168 | |
| D | LYS1168 | |
| D | LYS1171 | |
| A | LYS1171 | |
| B | LYS1168 | |
| B | LYS1171 | |
| C | LYS1168 | |
| C | LYS1171 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ARG1139 | |
| A | ASP1135 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP1135 | |
| B | ASN1140 | |
| B | ALA1137 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP1135 | |
| C | ASN1140 | |
| C | ALA1137 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP1135 | |
| D | ASN1140 | |
| D | ALA1137 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ARG1139 | |
| B | ASP1135 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ARG1139 | |
| C | ASP1135 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ARG1139 | |
| D | ASP1135 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP1135 | |
| A | ALA1137 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP1135 | |
| B | ALA1137 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP1135 | |
| C | ALA1137 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP1135 | |
| D | ALA1137 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP1135 | |
| A | ASN1140 | |
| A | ALA1137 |
