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 | ASP283 | |
B | ASP283 | |
Chain | Residue | Details |
A | LEU162 | |
A | LYS186 | |
B | LEU162 | |
B | LYS186 | |
Chain | Residue | Details |
A | SER135 | |
B | SER135 | |