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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | LYS159 |
| A | ASP294 |
| A | GLY296 |
| A | LEU297 |
| A | HOH739 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | ARG155 |
| A | THR160 |
| A | LYS218 |
| A | EDO503 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | THR160 |
| A | GLU177 |
| A | EDO502 |
| A | HOH610 |
| A | HOH616 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | SER252 |
| A | TRP253 |
| A | THR287 |
| A | GLY288 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | GLY285 |
| A | PRO286 |
| A | THR287 |
| A | GLY288 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | LYS307 |
| A | SER308 |
| A | GLY311 |
| A | MET316 |
| A | TYR321 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | GLU214 |
| A | TYR358 |
| A | THR362 |
| A | HOH650 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | VAL361 |
| A | ILE365 |
| A | LYS366 |
| A | ILE386 |
| A | GLN388 |
| A | HOH631 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | PRO313 |
| A | MET316 |
| A | TYR321 |
| A | ILE357 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 501 |
| Chain | Residue |
| B | LYS159 |
| B | ASP294 |
| B | GLY296 |
| B | LEU297 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | GLU177 |
| B | SER215 |
| B | ILE216 |
| B | HOH638 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | ASP180 |
| B | ARG181 |
| B | LEU183 |
| B | GLN188 |
| B | LYS220 |
| B | LYS221 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | LEU183 |
| B | GLU187 |
| B | ARG190 |
| B | PHE191 |
| B | GLU194 |
| B | THR299 |
| B | THR303 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| B | GLU214 |
| B | TYR358 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| B | TYR238 |
| B | PHE242 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| B | SER252 |
| B | TRP253 |
| B | THR287 |
| B | GLY288 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 508 |
| Chain | Residue |
| B | PRO313 |
| B | MET316 |
| B | PRO318 |
| B | TYR321 |
| B | ILE357 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 509 |
| Chain | Residue |
| B | PRO313 |
| B | GLU314 |
| B | CYS351 |
| B | GLN352 |
| B | HOH659 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKcdNIFI |
| Chain | Residue | Details |
| A | ILE271-ILE283 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9JIH7","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9H4A3","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q9JIH7","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"33439774","evidenceCode":"ECO:0000269"}]} |
