Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004712 | molecular_function | protein serine/threonine/tyrosine 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 | 16 |
Details | binding site for residue 7AA A 501 |
Chain | Residue |
A | ILE155 |
A | LEU231 |
A | SER232 |
A | ASN234 |
A | GLU279 |
A | LEU282 |
A | ILE294 |
A | EDO504 |
A | GLY156 |
A | LYS157 |
A | VAL163 |
A | ALA176 |
A | LYS178 |
A | ILE212 |
A | PHE228 |
A | GLU229 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | LYS165 |
A | HOH654 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | GLU363 |
A | LYS413 |
A | ARG415 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | ILE155 |
A | SER232 |
A | MET233 |
A | ASN234 |
A | 7AA501 |
A | HOH699 |
A | HOH710 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | HIS199 |
A | LYS202 |
B | ASP437 |
B | GLN441 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue EDO A 507 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO A 508 |
Chain | Residue |
A | PRO350 |
A | LYS413 |
A | ARG415 |
B | ARG411 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | SER104 |
A | TYR105 |
A | HOH633 |
site_id | AC9 |
Number of Residues | 16 |
Details | binding site for residue 7AA B 501 |
Chain | Residue |
B | ILE155 |
B | GLY156 |
B | LYS157 |
B | PHE160 |
B | VAL163 |
B | ALA176 |
B | LYS178 |
B | ILE212 |
B | PHE228 |
B | GLU229 |
B | LEU231 |
B | GLU279 |
B | LEU282 |
B | ILE294 |
B | ASP295 |
B | HOH673 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
A | LYS202 |
B | LEU436 |
B | LYS440 |
B | HOH646 |
B | HOH719 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | LYS277 |
B | GLU279 |
B | SER312 |
B | HOH605 |
B | HOH643 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
B | LYS386 |
B | TYR388 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGQVVkAydhkvhqh..........VALK |
Chain | Residue | Details |
A | ILE155-LYS178 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHcDLKpeNILL |
Chain | Residue | Details |
A | ILE271-LEU283 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP275 | |
B | ASP275 | |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | ILE155 | |
A | LYS178 | |
A | PHE228 | |
B | ILE155 | |
B | LYS178 | |
B | PHE228 | |
Chain | Residue | Details |
A | THR308 | |
B | THR308 | |
Chain | Residue | Details |
A | PTR309 | |
B | PTR309 | |
Chain | Residue | Details |
A | SER369 | |
B | SER369 | |
Chain | Residue | Details |
A | SER376 | |
B | SER376 | |