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 | 5 |
Details | binding site for residue BME A 801 |
Chain | Residue |
A | VAL547 |
A | CYS548 |
A | LYS692 |
A | GLU693 |
A | ARG694 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue BME B 801 |
Chain | Residue |
B | GLU693 |
B | ARG694 |
B | LEU536 |
B | VAL547 |
B | CYS548 |
B | LYS692 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 28 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGDGNFAVVKeCverstareyalk......IIKK |
Chain | Residue | Details |
A | ILE396-LYS423 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKpeNLLV |
Chain | Residue | Details |
A | ILE507-VAL519 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP511 | |
B | ASP511 | |
Chain | Residue | Details |
B | ILE396 | |
B | LYS419 | |
A | ILE396 | |
A | LYS419 | |
Chain | Residue | Details |
A | TYR520 | |
B | TYR520 | |