Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 601 |
| Chain | Residue |
| A | ASP394 |
| A | ASN396 |
| A | ASP398 |
| A | GLN400 |
| A | TYR447 |
| A | HOH545 |
| A | HOH546 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 602 |
| Chain | Residue |
| A | ILE195 |
| A | VAL196 |
| A | LEU223 |
| A | SER224 |
| A | ALA225 |
| A | HOH580 |
| A | GLU124 |
| A | ASN194 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1 |
| Chain | Residue |
| A | HOH6 |
| A | LYS105 |
| A | MET137 |
| A | LEU151 |
| A | MET153 |
| A | ASP220 |
| A | PHE221 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 538 |
| Chain | Residue |
| A | HOH11 |
| A | THR114 |
| A | SER116 |
| A | ASN117 |
| A | HOH644 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 539 |
| Chain | Residue |
| A | GLY119 |
| A | LEU122 |
| A | ASP123 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE J60 A 540 |
| Chain | Residue |
| A | LYS81 |
| A | LEU82 |
| A | ALA103 |
| A | MET137 |
| A | MET153 |
| A | GLU154 |
| A | VAL155 |
| A | TYR156 |
| A | LEU206 |
| A | ASP220 |
| A | ARG468 |
| A | GOL541 |
| A | GOL542 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 541 |
| Chain | Residue |
| A | HOH61 |
| A | ARG157 |
| A | GLY159 |
| A | LYS210 |
| A | J60540 |
| A | HOH560 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 542 |
| Chain | Residue |
| A | HOH63 |
| A | SER84 |
| A | GLU160 |
| A | GLU203 |
| A | LEU206 |
| A | VAL219 |
| A | J60540 |
| A | HOH674 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 543 |
| Chain | Residue |
| A | ASP253 |
| A | GLU254 |
| A | LYS255 |
| A | HOH570 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 544 |
| Chain | Residue |
| A | TYR87 |
| A | GLY88 |
| A | GLU89 |
| A | ILE106 |
| A | LYS108 |
| A | SER111 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 28 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAYGEVLlCkdkltgaeraik......IIKK |
| Chain | Residue | Details |
| A | LEU82-LYS109 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLL |
| Chain | Residue | Details |
| A | ILE195-LEU207 | |
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DNNGDGQLDrkEL |
| Chain | Residue | Details |
| A | ASP394-LEU406 | |
| A | ASP441-PHE453 | |
| A | ASP477-LEU489 | |
| A | ASP511-PHE523 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP199 | |
| A | GLU203 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP199 | |
| A | LYS201 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP199 | |
| A | LYS201 | |
| A | THR239 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN204 | |
| A | ASP199 | |
| A | LYS201 | |
