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 | 16 |
Details | BINDING SITE FOR RESIDUE STU A 1 |
Chain | Residue |
A | ILE557 |
A | GLY631 |
A | ARG635 |
A | PRO680 |
A | ASN681 |
A | LEU683 |
A | CYS693 |
A | ASP694 |
A | GLY558 |
A | VAL565 |
A | ALA576 |
A | LYS578 |
A | THR625 |
A | GLU626 |
A | TYR627 |
A | LEU628 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 22 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGSFGTVHrAewhgsd............VAVK |
Chain | Residue | Details |
A | ILE557-LYS578 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKspNLLV |
Chain | Residue | Details |
A | ILE672-VAL684 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP676 | |
B | ASP676 | |
Chain | Residue | Details |
A | ILE557 | |
A | LYS578 | |
B | ILE557 | |
B | LYS578 | |