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
| site_id | SWS_FT_FI1 |
| Number of Residues | 136 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q63470","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]} |
