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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | LYS264 |
| A | ARG300 |
| A | SER301 |
| A | HOH1046 |
| A | HOH1111 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | HOH715 |
| A | HOH1118 |
| A | ARG325 |
| A | ARG328 |
| A | GLU366 |
| A | HOH667 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | SER169 |
| A | LYS193 |
| A | LYS194 |
| A | HOH650 |
| A | HOH659 |
| A | HOH694 |
| A | HOH708 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | ASN144 |
| A | TYR145 |
| A | SER169 |
| A | LYS191 |
| A | LYS193 |
| A | HOH645 |
| A | HOH695 |
| A | HOH1145 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | LYS218 |
| A | TYR219 |
| A | ARG250 |
| A | HOH605 |
| A | HOH689 |
| A | HOH716 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | ASP454 |
| A | LEU457 |
| A | ARG458 |
| A | HOH894 |
| A | HOH986 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | ASN251 |
| A | THR252 |
| A | PRO279 |
| A | GLU280 |
| A | HOH641 |
| A | HOH681 |
| A | HOH718 |
| A | HOH923 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | SER258 |
| A | ASN260 |
| A | HOH1048 |
| A | HOH1081 |
| A | HOH1085 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | HIS223 |
| A | LYS225 |
| A | HOH1022 |
| A | HOH1148 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 510 |
| Chain | Residue |
| A | LYS175 |
| A | TYR472 |
| A | HOH614 |
| A | HOH619 |
| A | HOH652 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue EDO A 511 |
| Chain | Residue |
| A | GLN199 |
| A | GLN199 |
| A | ILE202 |
| A | ILE202 |
| A | TYR319 |
| A | TYR319 |
| A | HOH611 |
| A | HOH611 |
| A | HOH629 |
| A | HOH629 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 512 |
| Chain | Residue |
| A | LYS465 |
| A | THR466 |
| A | ARG467 |
| A | ILE468 |
| A | GLN469 |
| A | TYR472 |
| A | HOH603 |
| A | HOH652 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 513 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 514 |
| Chain | Residue |
| A | ARG226 |
| A | HOH957 |
| A | HOH1022 |
| A | HOH1097 |
| site_id | AD6 |
| Number of Residues | 12 |
| Details | binding site for residue 4E3 A 515 |
| Chain | Residue |
| A | GLY166 |
| A | LYS167 |
| A | PHE170 |
| A | ALA186 |
| A | LYS188 |
| A | PHE238 |
| A | GLU239 |
| A | LEU241 |
| A | LEU294 |
| A | ASP307 |
| A | HOH710 |
| A | HOH803 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q63470","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]} |
