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 | 15 |
Details | binding site for residue C5N A 901 |
Chain | Residue |
A | ILE531 |
A | TRP604 |
A | GLY605 |
A | ASP608 |
A | SER611 |
A | LEU654 |
A | ILE663 |
A | SER533 |
A | GLY534 |
A | SER537 |
A | ALA551 |
A | LYS553 |
A | ILE586 |
A | MET602 |
A | GLU603 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 902 |
Chain | Residue |
A | TRP622 |
A | LYS625 |
A | SER626 |
A | LYS629 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 23 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGSSKVFqVlnekkqi...........YAIK |
Chain | Residue | Details |
A | ILE531-LYS553 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHsDLKpaNFLI |
Chain | Residue | Details |
A | ILE643-ILE655 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP647 | |
Chain | Residue | Details |
A | ILE531 | |
A | LYS553 | |