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 | 7 |
Details | binding site for residue EDO A 501 |
Chain | Residue |
A | SER132 |
A | SER135 |
A | VAL145 |
A | ASP150 |
A | TRP151 |
A | HOH602 |
A | HOH607 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | GLU287 |
A | THR337 |
A | HIS339 |
A | HOH630 |
A | CYS146 |
A | ARG147 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | ARG199 |
A | ILE202 |
A | ASN203 |
A | LYS206 |
A | TRP225 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | GLU348 |
A | ARG402 |
A | HOH645 |
B | HIS330 |
B | HIS331 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | SER323 |
A | THR325 |
A | THR332 |
A | VAL335 |
A | HOH670 |
A | HOH731 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | ARG451 |
A | ALA458 |
A | GLN459 |
A | ARG460 |
A | GLU465 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | GLU454 |
A | GLN459 |
A | HOH779 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue EDO A 508 |
Chain | Residue |
A | ARG369 |
A | SER433 |
A | TYR434 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | GLU387 |
A | PRO392 |
A | ILE393 |
A | GLY411 |
A | LEU412 |
A | ASN417 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue CL A 510 |
Chain | Residue |
A | LYS403 |
A | LYS405 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue PO4 A 511 |
Chain | Residue |
A | ARG189 |
A | ARG189 |
A | LYS193 |
A | LYS193 |
A | TYR194 |
A | TYR194 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue EAE A 512 |
Chain | Residue |
A | LYS186 |
A | PHE236 |
A | GLU237 |
A | LEU238 |
A | LEU239 |
A | GLY240 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue PO4 B 501 |
Chain | Residue |
B | ARG189 |
B | ARG189 |
B | LYS193 |
B | LYS193 |
B | TYR194 |
B | TYR194 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
A | HOH770 |
B | ARG402 |
B | LYS403 |
B | LYS405 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | GLU378 |
B | LYS405 |
B | TYR406 |
B | HOH672 |
B | HOH773 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
B | GLU137 |
B | ASP138 |
B | ARG341 |
B | HOH735 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue EDO B 505 |
Chain | Residue |
B | ARG147 |
B | PHE244 |
B | PHE252 |
B | GLU366 |
B | GLY370 |
B | PHE371 |
B | THR372 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for residue EDO B 506 |
Chain | Residue |
B | PHE371 |
B | THR372 |
B | LEU373 |
B | GLN375 |
B | ASN427 |
B | CYS428 |
B | TYR434 |
B | HOH679 |
site_id | AE1 |
Number of Residues | 3 |
Details | binding site for residue EDO B 507 |
Chain | Residue |
B | PRO392 |
B | SER395 |
B | HOH625 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue EDO B 508 |
Chain | Residue |
A | HOH690 |
A | HOH782 |
B | ASP447 |
A | LYS432 |
A | VAL443 |
site_id | AE3 |
Number of Residues | 5 |
Details | binding site for residue EDO B 509 |
Chain | Residue |
B | GLN459 |
B | ARG460 |
B | GLU465 |
B | HOH604 |
B | HOH732 |
site_id | AE4 |
Number of Residues | 5 |
Details | binding site for residue EDO B 510 |
Chain | Residue |
B | GLU287 |
B | ASN288 |
B | LEU290 |
B | EAE512 |
B | HOH721 |
site_id | AE5 |
Number of Residues | 6 |
Details | binding site for residue GOL B 511 |
Chain | Residue |
A | THR332 |
A | THR333 |
A | HOH749 |
B | HIS330 |
B | THR333 |
B | HOH689 |
site_id | AE6 |
Number of Residues | 8 |
Details | binding site for residue EAE B 512 |
Chain | Residue |
B | LEU162 |
B | ALA184 |
B | LYS186 |
B | PHE236 |
B | LEU238 |
B | LEU239 |
B | GLY240 |
B | EDO510 |
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 | |