5Y86
Crystal structure of kinase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000242 | cellular_component | pericentriolar material |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005813 | cellular_component | centrosome |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0010494 | cellular_component | cytoplasmic stress granule |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016607 | cellular_component | nuclear speck |
| A | 0030218 | biological_process | erythrocyte differentiation |
| A | 0035063 | biological_process | nuclear speck organization |
| A | 0035617 | biological_process | stress granule disassembly |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0043518 | biological_process | negative regulation of DNA damage response, signal transduction by p53 class mediator |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051301 | biological_process | cell division |
| A | 0080135 | biological_process | regulation of cellular response to stress |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 1902751 | biological_process | positive regulation of cell cycle G2/M phase transition |
| A | 1903008 | biological_process | organelle disassembly |
| A | 1903432 | biological_process | regulation of TORC1 signaling |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue HRM A 601 |
| Chain | Residue |
| A | ALA236 |
| A | HOH735 |
| A | LYS238 |
| A | PHE288 |
| A | GLU289 |
| A | LEU290 |
| A | LEU291 |
| A | LEU342 |
| A | ILE354 |
| A | ASP355 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 602 |
| Chain | Residue |
| A | LYS151 |
| A | GLY218 |
| A | SER219 |
| A | LYS337 |
| A | HOH745 |
| A | HOH897 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 603 |
| Chain | Residue |
| A | ARG313 |
| A | LYS314 |
| A | LYS524 |
| A | HOH702 |
| A | HOH734 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 604 |
| Chain | Residue |
| A | ARG178 |
| A | LYS440 |
| A | TYR441 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 605 |
| Chain | Residue |
| A | LYS151 |
| A | LYS159 |
| A | PTR369 |
| A | ARG376 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 606 |
| Chain | Residue |
| A | ILE448 |
| A | PRO520 |
| A | SER523 |
| A | LYS524 |
| A | SER525 |
| A | HOH744 |
| A | HOH755 |
| A | HOH768 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 607 |
| Chain | Residue |
| A | ARG208 |
| A | PHE278 |
| A | HOH922 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 608 |
| Chain | Residue |
| A | SER308 |
| A | VAL309 |
| A | ARG461 |
| A | HOH947 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 609 |
| Chain | Residue |
| A | LEU343 |
| A | HIS346 |
| A | GLY347 |
| A | ARG348 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 610 |
| Chain | Residue |
| A | ARG450 |
| A | CYS452 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 611 |
| Chain | Residue |
| A | TYR296 |
| A | GLU297 |
| A | LYS300 |
| A | HOH707 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 612 |
| Chain | Residue |
| A | TYR157 |
| A | GLY180 |
| A | VAL181 |
| A | ILE182 |
| A | ASP413 |
| A | GLU414 |
| A | GLY415 |
| A | HOH704 |
| A | HOH927 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGQVArVydhklrqy..........VALK |
| Chain | Residue | Details |
| A | ILE215-LYS238 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHcDLKpeNILL |
| Chain | Residue | Details |
| A | ILE331-LEU343 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP335 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:29634919 |
| Chain | Residue | Details |
| A | ILE215 | |
| A | PHE288 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29634919 |
| Chain | Residue | Details |
| A | LYS238 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:29634919 |
| Chain | Residue | Details |
| A | SEP350 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q922Y0 |
| Chain | Residue | Details |
| A | PTR369 |
