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 | 10 |
| Details | binding site for residue JWN A 501 |
| Chain | Residue |
| A | ASN161 |
| A | ASP320 |
| A | LEU162 |
| A | ALA184 |
| A | LYS186 |
| A | PHE236 |
| A | GLU237 |
| A | LEU239 |
| A | GLY240 |
| A | LEU290 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | LEU218 |
| A | GLN266 |
| A | SER315 |
| A | ARG317 |
| A | PHE482 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | VAL145 |
| A | TRP151 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | PRO254 |
| A | GLU308 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | ASP327 |
| A | HIS328 |
| B | GLU416 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | ASP327 |
| A | GLU329 |
| A | HOH628 |
| B | ARG422 |
| B | LYS425 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | ARG451 |
| A | GLN459 |
| A | ILE461 |
| A | GLU465 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue JWN B 501 |
| Chain | Residue |
| B | ASN161 |
| B | LEU162 |
| B | ALA184 |
| B | LYS186 |
| B | GLU201 |
| B | PHE236 |
| B | GLU237 |
| B | LEU239 |
| B | GLY240 |
| B | LYS241 |
| B | LEU290 |
| B | ASP320 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | VAL413 |
| B | TRP414 |
| B | GLU416 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| A | ARG400 |
| B | HIS339 |
| B | GLN375 |
| B | THR376 |
| B | HIS377 |
| B | HOH612 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | ILE208 |
| B | ASN215 |
| B | CYS219 |
| B | VAL220 |
| B | LEU221 |
| B | MET222 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| B | TYR265 |
| B | HIS269 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGTFGKVVeCldhargksq.........VALK |
| Chain | Residue | Details |
| A | LEU162-LYS186 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF |
| Chain | Residue | Details |
| A | LEU279-PHE291 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | LEU431 | |
| B | LEU431 | |
| Chain | Residue | Details |
| A | SER310 | |
| A | ILE334 | |
| B | SER310 | |
| B | ILE334 | |
| Chain | Residue | Details |
| A | ARG155 | |
| B | ARG155 | |
| Chain | Residue | Details |
| A | GLU157 | |
| B | GLU157 | |
| Chain | Residue | Details |
| A | ALA197 | |
| A | ARG199 | |
| B | ALA197 | |
| B | ARG199 | |
| Chain | Residue | Details |
| A | ASN215 | |
| B | ASN215 | |
| Chain | Residue | Details |
| A | ASP224 | |
| A | PHE226 | |
| B | ASP224 | |
| B | PHE226 | |
| Chain | Residue | Details |
| A | ASP283 | |
| B | ASP283 | |
