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 |
| A | 0007163 | biological_process | establishment or maintenance of cell polarity |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007163 | biological_process | establishment or maintenance of cell polarity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue ADP A 601 |
| Chain | Residue |
| A | GLY261 |
| A | GLU333 |
| A | VAL335 |
| A | ASP339 |
| A | ASP382 |
| A | ASN383 |
| A | LEU385 |
| A | THR395 |
| A | ASP396 |
| A | PHE552 |
| A | MN603 |
| A | GLY263 |
| A | MN604 |
| A | AF3605 |
| F | ARG8 |
| A | SER264 |
| A | TYR265 |
| A | ALA266 |
| A | VAL268 |
| A | ALA281 |
| A | LYS283 |
| A | ILE332 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue AF3 A 602 |
| Chain | Residue |
| A | ARG377 |
| A | GLY415 |
| A | THR416 |
| A | TYR419 |
| A | ILE420 |
| A | ALA421 |
| A | ILE424 |
| A | VAL434 |
| A | ALA438 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MN A 603 |
| Chain | Residue |
| A | ASN383 |
| A | ASP396 |
| A | ADP601 |
| A | AF3605 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MN A 604 |
| Chain | Residue |
| A | ASP396 |
| A | ADP601 |
| A | AF3605 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue AF3 A 605 |
| Chain | Residue |
| A | SER264 |
| A | LYS380 |
| A | ASN383 |
| A | ASP396 |
| A | ADP601 |
| A | MN603 |
| A | MN604 |
| F | GLY10 |
| F | SER11 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue SCN A 606 |
| Chain | Residue |
| A | GLU288 |
| A | PRO565 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue MN A 607 |
| Chain | Residue |
| A | HIS354 |
| B | HIS354 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for residue ADP B 601 |
| Chain | Residue |
| B | GLY263 |
| B | SER264 |
| B | TYR265 |
| B | ALA266 |
| B | VAL268 |
| B | LYS283 |
| B | ILE332 |
| B | GLU333 |
| B | VAL335 |
| B | ASP339 |
| B | ASP382 |
| B | ASN383 |
| B | LEU385 |
| B | THR395 |
| B | ASP396 |
| B | PHE552 |
| B | MN603 |
| B | MN604 |
| B | AF3605 |
| G | ARG8 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue AF3 B 602 |
| Chain | Residue |
| B | ARG377 |
| B | ASP378 |
| B | TYR419 |
| B | ILE424 |
| B | VAL434 |
| B | ASP435 |
| B | ALA438 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 603 |
| Chain | Residue |
| B | LYS380 |
| B | ASN383 |
| B | ASP396 |
| B | ADP601 |
| B | AF3605 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MN B 604 |
| Chain | Residue |
| B | ASP396 |
| B | ADP601 |
| B | AF3605 |
| B | HOH705 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue AF3 B 605 |
| Chain | Residue |
| B | GLY263 |
| B | SER264 |
| B | TYR265 |
| B | LYS380 |
| B | ASN383 |
| B | ASP396 |
| B | ADP601 |
| B | MN603 |
| B | MN604 |
| G | GLY10 |
| G | SER11 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue SCN B 606 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 28 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGSYAKVLlVrlkktdriyamk......VVKK |
| Chain | Residue | Details |
| A | ILE260-LYS287 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKldNVLL |
| Chain | Residue | Details |
| A | ILE374-LEU386 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP378 | |
| B | ASP378 | |
| Chain | Residue | Details |
| A | ILE260 | |
| A | LYS283 | |
| B | ILE260 | |
| B | LYS283 | |
| Chain | Residue | Details |
| A | TYR265 | |
| B | TYR265 | |
| Chain | Residue | Details |
| A | TYR280 | |
| A | TYR334 | |
| B | TYR280 | |
| B | TYR334 | |
| Chain | Residue | Details |
| A | TPO412 | |
| B | TPO412 | |
| Chain | Residue | Details |
| A | TPO564 | |
| B | TPO564 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 756 |
| Chain | Residue | Details |
| A | ASP378 | proton shuttle (general acid/base) |
| A | LYS380 | electrostatic stabiliser |
| A | ASN383 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 756 |
| Chain | Residue | Details |
| B | ASP378 | proton shuttle (general acid/base) |
| B | LYS380 | electrostatic stabiliser |
| B | ASN383 | electrostatic stabiliser |
