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 0WB A 701 |
Chain | Residue |
A | VAL408 |
A | LEU473 |
A | LEU474 |
A | ASP521 |
A | ASN522 |
A | LEU524 |
A | ASP536 |
A | GLY411 |
A | VAL416 |
A | ALA429 |
A | VAL430 |
A | LYS431 |
A | GLU442 |
A | ILE469 |
A | MET471 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 25 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGSFGEVHrMkdkqtgfqc.........AVKK |
Chain | Residue | Details |
A | VAL408-LYS432 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHgDVKadNVLL |
Chain | Residue | Details |
A | ILE513-LEU525 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP517 | |
Chain | Residue | Details |
A | VAL408 | |
A | LYS431 | |
Chain | Residue | Details |
A | THR561 | |