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 | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | HOH114 |
| A | HOH116 |
| A | HOH121 |
| A | ACP300 |
| A | ASP1150 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ACP A 300 |
| Chain | Residue |
| A | HOH111 |
| A | HOH112 |
| A | HOH121 |
| A | HOH124 |
| A | HOH131 |
| A | HOH139 |
| A | HOH141 |
| A | MG301 |
| A | LEU1002 |
| A | GLN1004 |
| A | GLY1005 |
| A | SER1006 |
| A | VAL1010 |
| A | ALA1028 |
| A | LYS1030 |
| A | GLU1077 |
| A | MET1079 |
| A | MET1139 |
| A | ASP1150 |
| A | HOH48 |
| A | HOH65 |
| A | HOH96 |
| A | HOH100 |
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. DIYetaYYR |
| Chain | Residue | Details |
| A | ASP1156-ARG1164 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9312016","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18278056","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"38056462","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"27577745","evidenceCode":"ECO:0000269"}]} |
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 |
