Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE WCX A 1280 |
| Chain | Residue |
| A | ILE14 |
| A | ASP93 |
| A | ALA145 |
| A | PHE148 |
| A | GLY158 |
| A | ASP159 |
| A | PHE160 |
| A | HOH2216 |
| A | GLY15 |
| A | TYR19 |
| A | CYS22 |
| A | GLU87 |
| A | TYR88 |
| A | CYS89 |
| A | GLU90 |
| A | GLY92 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1282 |
| Chain | Residue |
| A | ASN154 |
| A | HIS277 |
| A | HIS279 |
| A | HOH2132 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 1288 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1283 |
| Chain | Residue |
| A | TYR207 |
| A | PRO215 |
| A | PHE233 |
| A | ARG234 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1284 |
| Chain | Residue |
| A | TYR181 |
| A | TYR182 |
| A | GLU208 |
| A | PRO214 |
| A | HOH2217 |
| A | HOH2219 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1285 |
| Chain | Residue |
| A | ASP242 |
| A | GLU243 |
| A | GLU246 |
| A | HIS277 |
| A | HIS279 |
| A | HOH2220 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1286 |
| Chain | Residue |
| A | LYS152 |
| A | GLN153 |
| A | HOH2131 |
| A | HOH2214 |
| A | HOH2221 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1287 |
| Chain | Residue |
| A | GLU195 |
| A | LYS196 |
| A | SER261 |
| A | VAL262 |
| A | HOH2117 |
| A | HOH2200 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1289 |
| Chain | Residue |
| A | ARG234 |
| A | ARG235 |
| A | LEU266 |
| A | HOH2166 |
| A | HOH2222 |
| A | HOH2224 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpaNVFL |
| Chain | Residue | Details |
| A | VAL137-LEU149 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000269"}]} |
