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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 351 A2001 |
Chain | Residue |
A | LEU1002 |
A | PHE1128 |
A | MET1139 |
A | ILE1148 |
A | GLY1149 |
A | ASP1150 |
A | HOH3155 |
A | ALA1028 |
A | LYS1030 |
A | GLU1047 |
A | MET1051 |
A | VAL1059 |
A | VAL1060 |
A | GLU1077 |
A | MET1079 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 351 B2001 |
Chain | Residue |
B | LEU1002 |
B | ALA1028 |
B | GLU1047 |
B | VAL1050 |
B | MET1051 |
B | VAL1060 |
B | MET1076 |
B | GLU1077 |
B | MET1079 |
B | GLY1082 |
B | PHE1128 |
B | MET1139 |
B | ILE1148 |
B | GLY1149 |
B | ASP1150 |
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 | LEU1002-LYS1030 | |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV |
Chain | Residue | Details |
A | PHE1128-VAL1140 | |
site_id | PS00239 |
Number of Residues | 9 |
Details | RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR |
Chain | Residue | Details |
A | ASP1156-ARG1164 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP1132 | |
B | ASP1132 | |
Chain | Residue | Details |
A | SER1006 | |
B | ASP1150 | |
A | LYS1030 | |
A | GLU1077 | |
A | ARG1136 | |
A | ASP1150 | |
B | SER1006 | |
B | LYS1030 | |
B | GLU1077 | |
B | ARG1136 | |
Chain | Residue | Details |
A | CYS1056 | |
B | CYS1056 | |
Chain | Residue | Details |
A | TYR1158 | |
A | TYR1162 | |
A | TYR1163 | |
B | TYR1158 | |
B | TYR1162 | |
B | TYR1163 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP1132 | |
A | ARG1136 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP1132 | |
B | ARG1136 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP1132 | |
A | ALA1134 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP1132 | |
B | ALA1134 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP1132 | |
A | ASN1137 | |
A | ALA1134 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP1132 | |
B | ASN1137 | |
B | ALA1134 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 246 |
Chain | Residue | Details |
A | ASP1132 | increase nucleophilicity, proton acceptor, proton donor, steric role |
A | ARG1136 | electrostatic stabiliser, increase electrophilicity, promote heterolysis |
A | ASN1137 | metal ligand |
A | ASP1150 | metal ligand |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 246 |
Chain | Residue | Details |
B | ASP1132 | increase nucleophilicity, proton acceptor, proton donor, steric role |
B | ARG1136 | electrostatic stabiliser, increase electrophilicity, promote heterolysis |
B | ASN1137 | metal ligand |
B | ASP1150 | metal ligand |