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 | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 536 |
| Chain | Residue |
| A | ASN199 |
| A | ASP212 |
| A | ATP535 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 538 |
| Chain | Residue |
| B | ASN199 |
| B | ASP212 |
| B | ATP537 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP A 535 |
| Chain | Residue |
| A | VAL86 |
| A | ALA99 |
| A | LYS101 |
| A | MET147 |
| A | GLU148 |
| A | MET150 |
| A | SER154 |
| A | GLN157 |
| A | ASP194 |
| A | LYS196 |
| A | SER198 |
| A | LEU201 |
| A | ASP212 |
| A | MG536 |
| A | 5EA1001 |
| A | LEU78 |
| A | GLY81 |
| A | ASN82 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP B 537 |
| Chain | Residue |
| B | LEU78 |
| B | GLY79 |
| B | GLY81 |
| B | ASN82 |
| B | GLY84 |
| B | ALA99 |
| B | LYS101 |
| B | MET147 |
| B | GLU148 |
| B | MET150 |
| B | SER154 |
| B | GLN157 |
| B | LYS196 |
| B | SER198 |
| B | ASN199 |
| B | LEU201 |
| B | ASP212 |
| B | MG538 |
| B | 5EA1002 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 5EA A 1001 |
| Chain | Residue |
| A | ASN82 |
| A | LYS101 |
| A | LEU119 |
| A | LEU122 |
| A | VAL131 |
| A | MET147 |
| A | ARG193 |
| A | ASP194 |
| A | ASP212 |
| A | PHE213 |
| A | GLY214 |
| A | VAL215 |
| A | SER216 |
| A | MET223 |
| A | ATP535 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 5EA B 1002 |
| Chain | Residue |
| B | LYS101 |
| B | LEU119 |
| B | LEU122 |
| B | VAL131 |
| B | ASP212 |
| B | PHE213 |
| B | GLY214 |
| B | VAL215 |
| B | SER216 |
| B | LEU219 |
| B | MET223 |
| B | ATP537 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVTkVqhrpsgli..........MARK |
| Chain | Residue | Details |
| A | LEU78-LYS101 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKpsNILV |
| Chain | Residue | Details |
| A | ILE190-VAL202 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP194 | |
| B | ASP194 | |
| Chain | Residue | Details |
| A | LEU78 | |
| A | LYS101 | |
| B | LEU78 | |
| B | LYS101 | |
| Chain | Residue | Details |
| A | SER222 | |
| B | SER222 | |
| Chain | Residue | Details |
| A | SER226 | |
| B | SER226 | |
| Chain | Residue | Details |
| A | SER293 | |
| B | SER293 | |
| Chain | Residue | Details |
| A | SER295 | |
| B | SER295 | |
| Chain | Residue | Details |
| A | SER306 | |
| B | SER306 | |
| Chain | Residue | Details |
| A | THR394 | |
| B | THR394 | |
| Chain | Residue | Details |
| A | THR396 | |
| B | THR396 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | SER198 | |
| A | ASP194 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | SER198 | |
| B | ASP194 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP194 | |
| A | LYS196 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP194 | |
| B | LYS196 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP194 | |
| A | THR230 | |
| A | LYS196 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP194 | |
| B | THR230 | |
| B | LYS196 | |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN199 | |
| A | ASP194 | |
| A | LYS196 | |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN199 | |
| B | ASP194 | |
| B | LYS196 | |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 282 |
| Chain | Residue | Details |
| A | ASP194 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP221 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 282 |
| Chain | Residue | Details |
| B | ASP194 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP221 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
