Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0007165 | biological_process | signal transduction |
| B | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0007165 | biological_process | signal transduction |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0007165 | biological_process | signal transduction |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0007165 | biological_process | signal transduction |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue KFD A 501 |
| Chain | Residue |
| A | MET192 |
| A | MET265 |
| A | PRO266 |
| A | GLY268 |
| A | ALA315 |
| A | ASN316 |
| A | LEU318 |
| A | ASP329 |
| A | HOH621 |
| A | HOH628 |
| A | HOH647 |
| A | GLY195 |
| A | VAL200 |
| A | ALA211 |
| A | LYS213 |
| A | VAL246 |
| A | TYR262 |
| A | VAL263 |
| A | TYR264 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue KFD B 501 |
| Chain | Residue |
| B | ILE185 |
| B | MET192 |
| B | GLY195 |
| B | GLY196 |
| B | VAL200 |
| B | ALA211 |
| B | LYS213 |
| B | VAL246 |
| B | TYR262 |
| B | VAL263 |
| B | TYR264 |
| B | MET265 |
| B | PRO266 |
| B | GLY268 |
| B | ASN316 |
| B | LEU318 |
| B | SER328 |
| B | ASP329 |
| B | HOH608 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue KFD C 501 |
| Chain | Residue |
| C | MET192 |
| C | PHE197 |
| C | VAL200 |
| C | ALA211 |
| C | LYS213 |
| C | VAL246 |
| C | TYR262 |
| C | VAL263 |
| C | TYR264 |
| C | MET265 |
| C | PRO266 |
| C | GLY268 |
| C | ALA315 |
| C | ASN316 |
| C | LEU318 |
| C | SER328 |
| C | ASP329 |
| C | HOH616 |
| C | HOH643 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | binding site for residue KFD D 501 |
| Chain | Residue |
| D | MET192 |
| D | GLU194 |
| D | GLY196 |
| D | VAL200 |
| D | ALA211 |
| D | LYS213 |
| D | VAL246 |
| D | TYR262 |
| D | VAL263 |
| D | TYR264 |
| D | MET265 |
| D | PRO266 |
| D | GLY268 |
| D | ALA315 |
| D | ASN316 |
| D | LEU318 |
| D | SER328 |
| D | ASP329 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | GLN435 | |
| B | GLN435 | |
| C | GLN435 | |
| D | GLN435 | |
| Chain | Residue | Details |
| A | ASN316 | |
| B | ASN316 | |
| C | ASN316 | |
| D | ASN316 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU337 | |
| D | GLU337 | |
| D | LEU437 | |
| D | LEU453 | |
| A | LEU437 | |
| A | LEU453 | |
| B | GLU337 | |
| B | LEU437 | |
| B | LEU453 | |
| C | GLU337 | |
| C | LEU437 | |
| C | LEU453 | |
