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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A 1 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 2 |
| Chain | Residue |
| A | CA1 |
| A | GLU1047 |
| A | 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 |
| B | GLN384 | |
| Chain | Residue | Details |
| B | ARG387 | |
| A | LYS1030 | |
| A | GLU1077 | |
| A | ARG1136 | |
| A | ASP1150 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305 |
| Chain | Residue | Details |
| A | TYR984 | |
| Chain | Residue | Details |
| A | CYS1056 | |
| Chain | Residue | Details |
| A | PTR1158 | |
| A | PTR1162 | |
| A | 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 |
| A | ASP1132 | |
| A | ALA1134 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP1132 | |
| A | ASN1137 | |
| A | 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 |
