Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine 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 | 9 |
Details | BINDING SITE FOR RESIDUE Y27 A 500 |
Chain | Residue |
A | VAL106 |
A | ALA119 |
A | GLU170 |
A | MET172 |
A | ASP218 |
A | ASN219 |
A | LEU221 |
A | ASP232 |
A | PHE384 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVQlVrhkasqkv..........YAMK |
Chain | Residue | Details |
A | ILE98-LYS121 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiHrDVKpdNMLL |
Chain | Residue | Details |
A | LEU210-LEU222 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP214 | |
Chain | Residue | Details |
A | ILE98 | |
A | LYS121 | |
Chain | Residue | Details |
A | THR414 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP218 | |
A | ASP214 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS216 | |
A | ASP214 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS216 | |
A | ASP214 | |
A | THR253 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS216 | |
A | ASN219 | |
A | ASP214 | |