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 |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue 4QG A 400 |
Chain | Residue |
A | VAL31 |
A | TYR36 |
A | ALA52 |
A | GLU106 |
A | PHE107 |
A | CYS108 |
A | ASP115 |
A | LEU160 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGNGTYGQVYkGrhvktgql..........AAIK |
Chain | Residue | Details |
A | VAL31-LYS54 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKgqNVLL |
Chain | Residue | Details |
A | VAL149-LEU161 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP153 | |
B | ASP153 | |
Chain | Residue | Details |
A | VAL31 | |
A | LYS54 | |
B | VAL31 | |
B | LYS54 | |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 | |
Chain | Residue | Details |
A | SER5 | |
B | SER5 | |