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 ATP A 601 |
| Chain | Residue |
| A | ILE251 |
| A | GLU324 |
| A | VAL326 |
| A | ASP387 |
| A | PHE543 |
| A | HOH706 |
| A | HOH714 |
| A | HOH732 |
| A | HOH736 |
| A | HOH738 |
| A | HOH742 |
| A | GLY252 |
| A | HOH794 |
| A | HOH804 |
| A | HOH847 |
| A | GLY254 |
| A | SER255 |
| A | TYR256 |
| A | ALA257 |
| A | VAL259 |
| A | LYS274 |
| A | ILE323 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP B 601 |
| Chain | Residue |
| B | ILE251 |
| B | GLY252 |
| B | ARG253 |
| B | GLY254 |
| B | SER255 |
| B | TYR256 |
| B | ALA257 |
| B | VAL259 |
| B | LYS274 |
| B | VAL307 |
| B | ILE323 |
| B | GLU324 |
| B | VAL326 |
| B | ASP387 |
| B | PHE543 |
| B | HOH703 |
| B | HOH718 |
| B | HOH728 |
| B | HOH779 |
| B | HOH835 |
| B | HOH836 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 611 |
| Chain | Residue |
| B | ARG337 |
| B | GLN338 |
| B | ARG441 |
| B | PRO473 |
| B | ARG474 |
| B | HOH752 |
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 | ILE251-LYS278 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKldNVLL |
| Chain | Residue | Details |
| A | ILE365-LEU377 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP369 | |
| B | ASP369 | |
| Chain | Residue | Details |
| A | ILE251 | |
| A | LYS274 | |
| B | ILE251 | |
| B | LYS274 | |
| Chain | Residue | Details |
| A | TYR256 | |
| B | TYR256 | |
| Chain | Residue | Details |
| A | TYR271 | |
| A | TYR325 | |
| B | TYR271 | |
| B | TYR325 | |
| Chain | Residue | Details |
| A | TPO403 | |
| B | TPO403 | |
| Chain | Residue | Details |
| A | TPO555 | |
| B | TPO555 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 756 |
| Chain | Residue | Details |
| A | ASP369 | proton shuttle (general acid/base) |
| A | LYS371 | electrostatic stabiliser |
| A | ASN374 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 756 |
| Chain | Residue | Details |
| B | ASP369 | proton shuttle (general acid/base) |
| B | LYS371 | electrostatic stabiliser |
| B | ASN374 | electrostatic stabiliser |
