Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue DXV A 501 |
| Chain | Residue |
| A | ILE134 |
| A | GLY236 |
| A | PRO237 |
| A | LEU282 |
| A | ASP293 |
| A | HOH605 |
| A | HOH614 |
| A | HOH616 |
| A | GLY137 |
| A | VAL142 |
| A | ALA155 |
| A | LYS157 |
| A | PHE230 |
| A | ASP231 |
| A | LEU232 |
| A | LEU233 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | VAL241 |
| A | CYS351 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue DXV B 501 |
| Chain | Residue |
| B | ILE134 |
| B | LYS136 |
| B | GLY137 |
| B | ALA155 |
| B | LYS157 |
| B | PHE230 |
| B | ASP231 |
| B | LEU232 |
| B | LEU233 |
| B | GLY236 |
| B | PRO237 |
| B | LEU282 |
| B | ASP293 |
| B | HOH606 |
| B | HOH611 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue DXV C 501 |
| Chain | Residue |
| C | ILE134 |
| C | GLY137 |
| C | VAL142 |
| C | ALA155 |
| C | LYS157 |
| C | PHE230 |
| C | ASP231 |
| C | LEU232 |
| C | LEU233 |
| C | GLY236 |
| C | PRO237 |
| C | ASN280 |
| C | LEU282 |
| C | ASP293 |
| C | HOH609 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue DXV D 501 |
| Chain | Residue |
| D | ILE134 |
| D | LYS136 |
| D | GLY137 |
| D | ALA155 |
| D | LYS157 |
| D | PHE230 |
| D | ASP231 |
| D | LEU233 |
| D | GLY236 |
| D | PRO237 |
| D | ASN280 |
| D | LEU282 |
| D | ASP293 |
| D | HOH601 |
| D | HOH606 |
| D | HOH612 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGAYGVVRlAynesedrh..........YAMK |
| Chain | Residue | Details |
| A | ILE134-LYS157 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKpsNLLL |
| Chain | Residue | Details |
| A | ILE271-LEU283 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
