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 | 13 |
Details | binding site for residue 9JS A 501 |
Chain | Residue |
A | ILE171 |
A | HOH609 |
A | HOH685 |
A | HOH705 |
A | HOH707 |
A | VAL179 |
A | ALA192 |
A | LYS194 |
A | LEU269 |
A | VAL270 |
A | GLN272 |
A | SER367 |
A | HOH604 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 502 |
Chain | Residue |
A | HOH602 |
A | HOH608 |
A | HOH618 |
A | HOH631 |
A | HOH677 |
A | HOH679 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSYGVVKlAynendnty..........YAMK |
Chain | Residue | Details |
A | ILE171-LYS194 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDIKpsNLLV |
Chain | Residue | Details |
A | ILE308-VAL320 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP312 | |
Chain | Residue | Details |
A | ILE171 | |
A | LYS194 | |