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 | 0005509 | molecular_function | calcium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0016020 | cellular_component | membrane |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0016020 | cellular_component | membrane |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 501 |
| Chain | Residue |
| A | ASP345 |
| A | ASN347 |
| A | ASP349 |
| A | GLN351 |
| A | GLU356 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | GLU400 |
| A | GLU403 |
| A | ASP392 |
| A | ASP394 |
| A | ASN396 |
| A | PHE398 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 503 |
| Chain | Residue |
| A | ASP428 |
| A | ASP430 |
| A | SER432 |
| A | LYS434 |
| A | GLU439 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 504 |
| Chain | Residue |
| A | ASP462 |
| A | ASN464 |
| A | ASP466 |
| A | GLU468 |
| A | GLU473 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 505 |
| Chain | Residue |
| A | ASN156 |
| A | ASP172 |
| A | ADP506 |
| A | HOH601 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue ADP A 506 |
| Chain | Residue |
| A | GLY35 |
| A | GLY37 |
| A | SER38 |
| A | VAL42 |
| A | ALA55 |
| A | LYS57 |
| A | GLU106 |
| A | TYR108 |
| A | GLU112 |
| A | GLU155 |
| A | ASN156 |
| A | LEU158 |
| A | ILE171 |
| A | ASP172 |
| A | MG505 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 501 |
| Chain | Residue |
| B | ASP345 |
| B | ASN347 |
| B | ASP349 |
| B | GLN351 |
| B | GLU356 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 502 |
| Chain | Residue |
| B | ASP392 |
| B | ASP394 |
| B | ASN396 |
| B | PHE398 |
| B | GLU400 |
| B | GLU403 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 503 |
| Chain | Residue |
| B | ASP428 |
| B | ASP430 |
| B | SER432 |
| B | LYS434 |
| B | GLU439 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 504 |
| Chain | Residue |
| B | ASP462 |
| B | ASN464 |
| B | ASP466 |
| B | GLU468 |
| B | GLU473 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 505 |
| Chain | Residue |
| B | ASN156 |
| B | ASP172 |
| B | ADP506 |
| B | HOH601 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for residue ADP B 506 |
| Chain | Residue |
| B | GLY35 |
| B | GLY37 |
| B | SER38 |
| B | VAL42 |
| B | ALA55 |
| B | LYS57 |
| B | GLU106 |
| B | TYR108 |
| B | GLU112 |
| B | GLU155 |
| B | ASN156 |
| B | LEU158 |
| B | ILE171 |
| B | ASP172 |
| B | MG505 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DKNGDGQLDkqEL |
| Chain | Residue | Details |
| A | ASP345-LEU357 | |
| A | ASP392-PHE404 | |
| A | ASP428-LEU440 | |
| A | ASP462-PHE474 | |
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGSFGEVIlCkdkvtgqe..........YAVK |
| Chain | Residue | Details |
| A | LEU34-LYS57 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLL |
| Chain | Residue | Details |
| A | ILE147-LEU159 | |
