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 WGZ A 1280 |
Chain | Residue |
A | ILE14 |
A | ALA145 |
A | PHE148 |
A | GLY158 |
A | ASP159 |
A | LEU162 |
A | LEU166 |
A | HOH2245 |
A | GLY15 |
A | CYS22 |
A | LYS37 |
A | GLU87 |
A | TYR88 |
A | CYS89 |
A | ASP93 |
A | SER96 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1281 |
Chain | Residue |
A | LEU11 |
A | LYS152 |
A | GLN153 |
A | HOH2241 |
A | HOH2246 |
A | HOH2247 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 1282 |
Chain | Residue |
A | ILE247 |
A | GLU264 |
A | ASN268 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1283 |
Chain | Residue |
A | ASP242 |
A | GLU243 |
A | GLU246 |
A | HIS277 |
A | HIS279 |
A | HOH2249 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1284 |
Chain | Residue |
A | TYR238 |
A | ARG239 |
A | SER241 |
A | HOH2250 |
A | HOH2251 |
A | HOH2252 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 1285 |
Chain | Residue |
A | TYR12 |
A | ARG115 |
A | GLN153 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 1286 |
Chain | Residue |
A | ARG234 |
A | ARG235 |
A | TYR238 |
A | LEU266 |
A | HOH2230 |
A | HOH2254 |
A | HOH2255 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1287 |
Chain | Residue |
A | TYR181 |
A | TYR182 |
A | GLU208 |
A | PRO214 |
A | HOH2257 |
A | HOH2258 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1288 |
Chain | Residue |
A | GLU195 |
A | LYS196 |
A | SER261 |
A | VAL262 |
A | HOH2223 |
A | HOH2259 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 1290 |
Chain | Residue |
A | GLU110 |
A | ARG239 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 1292 |
Chain | Residue |
A | ASN154 |
A | HIS277 |
A | HOH2150 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS A 1291 |
Chain | Residue |
A | HIS128 |
A | ARG130 |
A | TYR193 |
A | ASN194 |
A | GLU195 |
A | ASP198 |
A | HOH2260 |
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 | 8 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000269"}]} |