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 | 14 |
Details | binding site for residue 98G A 601 |
Chain | Residue |
A | ILE305 |
A | GLY382 |
A | PHE433 |
A | ASP463 |
A | HOH718 |
A | HOH732 |
A | PHE310 |
A | VAL313 |
A | ALA326 |
A | VAL360 |
A | ASN376 |
A | GLU377 |
A | TYR378 |
A | CYS379 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue CL A 602 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 603 |
Chain | Residue |
A | ARG329 |
A | HIS371 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGEFGSVFkCvkrldgci..........YAIK |
Chain | Residue | Details |
A | ILE305-LYS328 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LvHmDIKpsNIFI |
Chain | Residue | Details |
A | LEU422-ILE434 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP426 | |
Chain | Residue | Details |
A | ILE305 | |
A | LYS328 | |
Chain | Residue | Details |
A | ASN342 | |
A | ASN431 | |
A | ASP463 | |
A | GLY465 | |
Chain | Residue | Details |
A | SER307 | |
Chain | Residue | Details |
A | SER312 | |