Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine 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 | 15 |
Details | binding site for residue F7D A 401 |
Chain | Residue |
A | ILE17 |
A | CYS89 |
A | PRO90 |
A | GLY92 |
A | LEU139 |
A | ILE149 |
A | HOH509 |
A | VAL25 |
A | ALA38 |
A | LYS40 |
A | ASN45 |
A | CYS70 |
A | LEU86 |
A | GLU87 |
A | TYR88 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | GLU6 |
A | TYR10 |
A | HIS74 |
A | ASP311 |
A | HIS312 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGTGGFAKVKlAchiltgem..........VAIK |
Chain | Residue | Details |
A | ILE17-LYS40 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YaHrDLKpeNLLF |
Chain | Residue | Details |
A | TYR128-PHE140 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP132 | |
Chain | Residue | Details |
A | ILE17 | |
A | LYS40 | |
Chain | Residue | Details |
A | THR56 | |
Chain | Residue | Details |
A | TYR163 | |
Chain | Residue | Details |
A | THR167 | |
Chain | Residue | Details |
A | SER171 | |
A | SER253 | |
A | SER336 | |