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 | 2 |
Details | BINDING SITE FOR RESIDUE CA A 1306 |
Chain | Residue |
A | HIS285 |
B | HIS285 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 1304 |
Chain | Residue |
A | LYS52 |
A | THR164 |
A | ASP165 |
A | PHE166 |
A | SER169 |
A | J601305 |
A | HOH2088 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE J60 A 1305 |
Chain | Residue |
A | LEU29 |
A | VAL37 |
A | ALA50 |
A | LYS52 |
A | MET98 |
A | GLN99 |
A | LEU100 |
A | VAL101 |
A | LEU151 |
A | THR164 |
A | ASP165 |
A | EDO1304 |
B | TYR236 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 1303 |
Chain | Residue |
B | LYS52 |
B | THR164 |
B | ASP165 |
B | PHE166 |
B | J601305 |
B | HOH2149 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO B 1304 |
Chain | Residue |
A | ASP144 |
A | VAL201 |
A | SER205 |
A | HOH2079 |
A | HOH2103 |
B | ILE176 |
B | TYR186 |
B | VAL187 |
B | ALA188 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE J60 B 1305 |
Chain | Residue |
B | LEU29 |
B | VAL37 |
B | ALA50 |
B | MET98 |
B | GLN99 |
B | LEU100 |
B | VAL101 |
B | THR164 |
B | ASP165 |
B | EDO1303 |
B | HOH2150 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 28 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFSEVFlVkqrltgklfalk......CIKK |
Chain | Residue | Details |
A | LEU29-LYS56 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLY |
Chain | Residue | Details |
A | ILE140-TYR152 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP144 | |
B | ASP144 | |
Chain | Residue | Details |
A | LEU29 | |
A | LYS52 | |
B | LEU29 | |
B | LYS52 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | GLU148 | |
A | ASP144 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | GLU148 | |
B | ASP144 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP144 | |
A | LYS146 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP144 | |
B | LYS146 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR183 | |
A | ASP144 | |
A | LYS146 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | THR183 | |
B | ASP144 | |
B | LYS146 | |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASN149 | |
A | ASP144 | |
A | LYS146 | |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASN149 | |
B | ASP144 | |
B | LYS146 | |