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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 501 |
| Chain | Residue |
| A | SER384 |
| A | LYS410 |
| A | TYR411 |
| B | LYS410 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 502 |
| Chain | Residue |
| A | HIS335 |
| A | SER337 |
| A | THR338 |
| B | HIS335 |
| B | THR338 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 503 |
| Chain | Residue |
| A | ARG343 |
| A | HIS382 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | PHE251 |
| A | ASN255 |
| A | PRO259 |
| A | PHE260 |
| A | ARG261 |
| A | HIS264 |
| A | ARG314 |
| A | THR315 |
| A | LEU316 |
| A | HOH608 |
| A | HOH609 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue PQ5 A 505 |
| Chain | Residue |
| A | LEU167 |
| A | ALA189 |
| A | LYS191 |
| A | GLU206 |
| A | PHE241 |
| A | GLU242 |
| A | LEU244 |
| A | GLY245 |
| A | GLU292 |
| A | ASN293 |
| A | LEU295 |
| A | ASP325 |
| A | HOH623 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue PQ5 B 501 |
| Chain | Residue |
| B | LEU167 |
| B | ALA189 |
| B | LYS191 |
| B | GLU206 |
| B | PHE241 |
| B | GLU242 |
| B | LEU244 |
| B | GLY245 |
| B | GLU292 |
| B | LEU295 |
| B | VAL324 |
| B | ASP325 |
| B | HOH610 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 C 501 |
| Chain | Residue |
| C | SER384 |
| C | LYS410 |
| C | TYR411 |
| C | HOH653 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue PQ5 C 502 |
| Chain | Residue |
| C | LEU167 |
| C | ALA189 |
| C | LYS191 |
| C | GLU206 |
| C | PHE241 |
| C | GLU242 |
| C | LEU244 |
| C | GLY245 |
| C | LEU295 |
| C | VAL324 |
| C | ASP325 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVVeCidhkaggrh.........VAVK |
| Chain | Residue | Details |
| A | LEU167-LYS191 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF |
| Chain | Residue | Details |
| A | LEU284-PHE296 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 948 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| 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_FI3 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
