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 | 12 |
Details | binding site for residue P48 A 401 |
Chain | Residue |
A | TYR121 |
A | PHE240 |
A | ASP251 |
A | HOH647 |
A | VAL124 |
A | ALA137 |
A | LYS139 |
A | THR187 |
A | GLU188 |
A | CYS190 |
A | GLY191 |
A | GLN196 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue PEG A 402 |
Chain | Residue |
A | SER114 |
A | ARG115 |
A | GLN313 |
A | HOH532 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGHGSYGEVFkVrskedgrl..........YAVK |
Chain | Residue | Details |
A | LEU116-LYS139 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LvHlDVKpaNIFL |
Chain | Residue | Details |
A | LEU229-LEU241 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP233 | |
Chain | Residue | Details |
A | LEU116 | |
A | LYS139 | |
Chain | Residue | Details |
A | ASN238 | |
A | ASP251 | |
A | GLY253 | |
Chain | Residue | Details |
A | SER94 | |
Chain | Residue | Details |
A | SER120 | |
Chain | Residue | Details |
A | SER143 | |
Chain | Residue | Details |
A | SER160 | |