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 | 11 |
Details | binding site for residue H3E A 501 |
Chain | Residue |
A | LEU167 |
A | LEU295 |
A | HOH653 |
A | PHE172 |
A | ALA189 |
A | LYS191 |
A | PHE241 |
A | GLU242 |
A | LEU244 |
A | GLY245 |
A | GLU292 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | HIS233 |
A | HIS234 |
A | HOH612 |
A | HOH621 |
A | HOH774 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | SER220 |
A | LYS322 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | ARG160 |
A | HOH605 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | LEU243 |
A | LEU244 |
A | VAL297 |
A | GLN298 |
A | SER299 |
A | EDO506 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | LEU244 |
A | GLY245 |
A | LEU246 |
A | EDO505 |
A | HOH644 |
A | HOH648 |
A | HOH723 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | ILE252 |
A | ASN255 |
A | LEU258 |
A | PRO259 |
A | PHE260 |
A | HOH622 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue EDO A 508 |
Chain | Residue |
A | PRO259 |
A | PHE260 |
A | ARG261 |
A | LEU262 |
A | TYR373 |
A | LEU441 |
A | EDO509 |
A | HOH618 |
A | HOH710 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | PRO259 |
A | EDO508 |
A | HOH618 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO A 510 |
Chain | Residue |
A | LEU262 |
A | ASP263 |
A | ARG266 |
A | GLU446 |
A | HOH731 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 511 |
Chain | Residue |
A | MET440 |
A | LEU441 |
A | SER442 |
A | GLN443 |
A | HOH771 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue EDO A 512 |
Chain | Residue |
A | TRP419 |
A | ASP420 |
A | SER423 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 513 |
Chain | Residue |
A | CYS200 |
A | GLU201 |
A | ARG204 |
A | LYS385 |
A | LYS410 |
A | TYR411 |
A | HOH893 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 25 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVVeCidhkaggrh.........VAVK |
Chain | Residue | Details |
A | LEU167-LYS191 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF |
Chain | Residue | Details |
A | LEU284-PHE296 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP288 | |
Chain | Residue | Details |
A | LEU167 | |
A | LYS191 | |