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 | 12 |
Details | binding site for residue X7Y A 701 |
Chain | Residue |
A | ILE396 |
A | ASP533 |
A | HOH835 |
A | HOH844 |
A | GLU406 |
A | ALA417 |
A | MET465 |
A | GLU466 |
A | VAL468 |
A | LYS469 |
A | GLU515 |
A | LEU518 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue X7Y B 701 |
Chain | Residue |
B | ILE396 |
B | GLU406 |
B | VAL449 |
B | MET465 |
B | GLU466 |
B | LEU467 |
B | VAL468 |
B | GLY471 |
B | GLU515 |
B | LEU518 |
B | HOH805 |
B | HOH822 |
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 |
A | ILE396 | |
A | LYS419 | |
B | ILE396 | |
B | LYS419 | |
Chain | Residue | Details |
A | SER376 | |
B | SER376 | |
Chain | Residue | Details |
A | TYR520 | |
B | TYR520 | |