Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0046777 | biological_process | protein autophosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0046777 | biological_process | protein autophosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0046777 | biological_process | protein autophosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0046777 | biological_process | protein autophosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | LYS422 |
| A | LEU423 |
| A | HIS424 |
| A | LYS453 |
| D | ARG458 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | ARG255 |
| A | SER258 |
| A | ARG438 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PG4 A 503 |
| Chain | Residue |
| A | HIS227 |
| A | HOH625 |
| B | GLN201 |
| B | HIS227 |
| A | GLN201 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue PG4 A 504 |
| Chain | Residue |
| A | LYS175 |
| A | TRP184 |
| A | MET240 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 505 |
| Chain | Residue |
| A | ARG467 |
| A | ILE468 |
| A | GLN469 |
| A | TYR472 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue JHW A 506 |
| Chain | Residue |
| A | PHE170 |
| A | LYS188 |
| A | GLU239 |
| A | LEU241 |
| A | SER242 |
| A | LEU294 |
| A | VAL306 |
| A | ASP307 |
| A | HOH649 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 501 |
| Chain | Residue |
| B | LYS264 |
| B | ARG300 |
| B | SER301 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | SER258 |
| B | ASN260 |
| B | HOH604 |
| B | HOH612 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | ARG255 |
| B | GLY256 |
| B | ARG438 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue PG4 B 504 |
| Chain | Residue |
| B | LYS175 |
| B | TRP184 |
| B | MET240 |
| B | JHW508 |
| B | HOH605 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 505 |
| Chain | Residue |
| B | LEU261 |
| B | PRO298 |
| B | LYS299 |
| B | ARG300 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 506 |
| Chain | Residue |
| B | HIS424 |
| B | LYS453 |
| B | ARG458 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 507 |
| Chain | Residue |
| B | ILE468 |
| B | GLN469 |
| B | TYR472 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue JHW B 508 |
| Chain | Residue |
| B | PHE170 |
| B | LYS188 |
| B | GLU239 |
| B | LEU241 |
| B | SER242 |
| B | LEU294 |
| B | VAL306 |
| B | ASP307 |
| B | PG4504 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 501 |
| Chain | Residue |
| C | LYS264 |
| C | ARG300 |
| C | SER301 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 502 |
| Chain | Residue |
| C | ARG458 |
| C | ARG467 |
| C | ILE468 |
| C | GLN469 |
| C | TYR472 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue PG4 C 503 |
| Chain | Residue |
| C | GLN201 |
| C | HIS227 |
| D | GLN201 |
| D | HIS227 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue EPE C 504 |
| Chain | Residue |
| C | ASN260 |
| C | LYS264 |
| C | LYS299 |
| C | ARG300 |
| C | SER301 |
| C | HOH605 |
| C | HOH606 |
| site_id | AE1 |
| Number of Residues | 11 |
| Details | binding site for residue JHW C 505 |
| Chain | Residue |
| C | ILE165 |
| C | PHE170 |
| C | ALA186 |
| C | LYS188 |
| C | GLU239 |
| C | MET240 |
| C | LEU241 |
| C | SER242 |
| C | LEU294 |
| C | VAL306 |
| C | ASP307 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 501 |
| Chain | Residue |
| D | LYS264 |
| D | ARG300 |
| D | SER301 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 502 |
| Chain | Residue |
| D | GLN469 |
| D | TYR472 |
| D | HOH616 |
| D | ARG458 |
| D | ARG467 |
| D | ILE468 |
| site_id | AE4 |
| Number of Residues | 4 |
| Details | binding site for residue PG4 D 503 |
| Chain | Residue |
| D | ASP162 |
| D | LYS175 |
| D | TRP184 |
| D | MET240 |
| site_id | AE5 |
| Number of Residues | 8 |
| Details | binding site for residue JHW D 504 |
| Chain | Residue |
| D | PHE170 |
| D | LYS188 |
| D | GLU239 |
| D | LEU241 |
| D | SER242 |
| D | LEU294 |
| D | ASP307 |
| D | HOH625 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGQVVkAydrveqew..........VAIK |
| Chain | Residue | Details |
| A | ILE165-LYS188 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHcDLKpeNILL |
| Chain | Residue | Details |
| A | ILE283-LEU295 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP287 | |
| B | ASP287 | |
| C | ASP287 | |
| D | ASP287 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | ILE165 | |
| D | ILE165 | |
| D | LYS188 | |
| D | PHE238 | |
| A | LYS188 | |
| A | PHE238 | |
| B | ILE165 | |
| B | LYS188 | |
| B | PHE238 | |
| C | ILE165 | |
| C | LYS188 | |
| C | PHE238 | |
| Chain | Residue | Details |
| A | TYR140 | |
| B | TYR319 | |
| B | PTR321 | |
| B | TYR449 | |
| C | TYR140 | |
| C | TYR159 | |
| C | TYR177 | |
| C | TYR319 | |
| C | PTR321 | |
| C | TYR449 | |
| D | TYR140 | |
| A | TYR159 | |
| D | TYR159 | |
| D | TYR177 | |
| D | TYR319 | |
| D | PTR321 | |
| D | TYR449 | |
| A | TYR177 | |
| A | TYR319 | |
| A | PTR321 | |
| A | TYR449 | |
| B | TYR140 | |
| B | TYR159 | |
| B | TYR177 | |
| Chain | Residue | Details |
| A | TYR145 | |
| B | TYR145 | |
| C | TYR145 | |
| D | TYR145 | |
| Chain | Residue | Details |
| A | TYR219 | |
| B | TYR219 | |
| C | TYR219 | |
| D | TYR219 | |
| Chain | Residue | Details |
| A | SER310 | |
| B | SER310 | |
| C | SER310 | |
| D | SER310 | |
| Chain | Residue | Details |
| A | THR402 | |
| B | THR402 | |
| C | THR402 | |
| D | THR402 | |
