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 | 4 |
Details | BINDING SITE FOR RESIDUE MG A 201 |
Chain | Residue |
A | ASN1137 |
A | ASP1150 |
B | HOH1 |
B | 112101 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 202 |
Chain | Residue |
A | HOH21 |
A | HOH22 |
A | ASP1150 |
B | HOH20 |
B | 112101 |
site_id | AC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE 112 B 101 |
Chain | Residue |
A | MG201 |
A | MG202 |
A | LEU1002 |
A | GLY1005 |
A | SER1006 |
A | VAL1010 |
A | ALA1028 |
A | LYS1030 |
A | GLU1077 |
A | MET1079 |
A | ASP1083 |
A | ASP1132 |
A | ARG1136 |
A | ASN1137 |
A | ASP1150 |
B | HOH1 |
B | HOH14 |
B | HOH20 |
B | PRO102 |
B | ALA103 |
B | PHE107 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR CHAIN B OF BISUBSTRATE PEPTIDE INHIBITOR |
Chain | Residue |
A | GLN1004 |
A | GLU1094 |
A | ARG1136 |
A | GLY1167 |
A | LYS1168 |
A | GLY1169 |
A | LEU1170 |
A | LEU1171 |
A | PRO1172 |
A | VAL1173 |
A | TRP1175 |
A | LEU1181 |
A | LYS1182 |
A | ASP1183 |
A | GLY1184 |
A | ASN1215 |
A | ASP1232 |
B | HOH6 |
B | 112101 |
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 | |
Chain | Residue | Details |
A | SER1006 | |
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 | PHE984 | |
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 |