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 | 0007165 | biological_process | signal transduction |
| C | 0035591 | molecular_function | signaling adaptor activity |
| D | 0007165 | biological_process | signal transduction |
| D | 0035591 | molecular_function | signaling adaptor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 201 |
| Chain | Residue |
| A | HOH63 |
| A | ASN1137 |
| A | ASP1150 |
| E | 112117 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 202 |
| Chain | Residue |
| B | ASN1137 |
| B | ASP1150 |
| F | HOH66 |
| F | 112117 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 112 E 117 |
| Chain | Residue |
| A | MN201 |
| A | GLN1004 |
| A | GLY1005 |
| A | SER1006 |
| A | VAL1010 |
| A | ALA1028 |
| A | LYS1030 |
| A | MET1076 |
| A | GLU1077 |
| A | MET1079 |
| A | ASP1083 |
| A | ASP1132 |
| A | ARG1136 |
| A | ASN1137 |
| A | MET1139 |
| A | ASP1150 |
| E | HOH62 |
| E | HOH64 |
| E | ALA104 |
| E | PHE108 |
| A | HOH63 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 112 F 117 |
| Chain | Residue |
| B | MN202 |
| B | GLN1004 |
| B | GLY1005 |
| B | SER1006 |
| B | VAL1010 |
| B | ALA1028 |
| B | LYS1030 |
| B | MET1076 |
| B | GLU1077 |
| B | MET1079 |
| B | ASP1132 |
| B | ARG1136 |
| B | ASN1137 |
| B | MET1139 |
| B | ASP1150 |
| F | HOH11 |
| F | HOH66 |
| F | PHE108 |
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 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305 |
| Chain | Residue | Details |
| A | TYR984 | |
| B | TYR984 | |
| Chain | Residue | Details |
| A | CYS1056 | |
| B | CYS1056 | |
| Chain | Residue | Details |
| A | PTR1158 | |
| A | PTR1162 | |
| A | PTR1163 | |
| B | PTR1158 | |
| B | PTR1162 | |
| B | PTR1163 | |
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 |
