7Z5N
Crystal structure of DYRK1A in complex with CX-4945
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 |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
| E | 0046777 | biological_process | protein autophosphorylation |
| F | 0004672 | molecular_function | protein kinase activity |
| F | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006468 | biological_process | protein phosphorylation |
| F | 0046777 | biological_process | protein autophosphorylation |
| G | 0004672 | molecular_function | protein kinase activity |
| G | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006468 | biological_process | protein phosphorylation |
| G | 0046777 | biological_process | protein autophosphorylation |
| H | 0004672 | molecular_function | protein kinase activity |
| H | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0006468 | biological_process | protein phosphorylation |
| H | 0046777 | biological_process | protein autophosphorylation |
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 | 8 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:23665168 |
| Chain | Residue | Details |
| A | ASP287 | |
| B | ASP287 | |
| C | ASP287 | |
| D | ASP287 | |
| E | ASP287 | |
| F | ASP287 | |
| G | ASP287 | |
| H | ASP287 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | ILE165 | |
| A | LYS188 | |
| A | PHE238 | |
| B | ILE165 | |
| B | LYS188 | |
| B | PHE238 | |
| C | ILE165 | |
| C | LYS188 | |
| C | PHE238 | |
| D | ILE165 | |
| D | LYS188 | |
| D | PHE238 | |
| E | ILE165 | |
| E | LYS188 | |
| E | PHE238 | |
| F | ILE165 | |
| F | LYS188 | |
| F | PHE238 | |
| G | ILE165 | |
| G | LYS188 | |
| G | PHE238 | |
| H | ILE165 | |
| H | LYS188 | |
| H | PHE238 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:23665168 |
| Chain | Residue | Details |
| A | TYR140 | |
| A | TYR159 | |
| A | TYR177 | |
| A | TYR319 | |
| A | PTR321 | |
| A | TYR449 | |
| B | TYR140 | |
| B | TYR159 | |
| B | TYR177 | |
| B | TYR319 | |
| B | PTR321 | |
| B | TYR449 | |
| C | TYR140 | |
| C | TYR159 | |
| C | TYR177 | |
| C | TYR319 | |
| C | PTR321 | |
| C | TYR449 | |
| D | TYR140 | |
| D | TYR159 | |
| D | TYR177 | |
| D | TYR319 | |
| D | PTR321 | |
| D | TYR449 | |
| E | TYR140 | |
| E | TYR159 | |
| E | TYR177 | |
| E | TYR319 | |
| E | PTR321 | |
| E | TYR449 | |
| F | TYR140 | |
| F | TYR159 | |
| F | TYR177 | |
| F | TYR319 | |
| F | PTR321 | |
| F | TYR449 | |
| G | TYR140 | |
| G | TYR159 | |
| G | TYR177 | |
| G | TYR319 | |
| G | PTR321 | |
| G | TYR449 | |
| H | TYR140 | |
| H | TYR159 | |
| H | TYR177 | |
| H | TYR319 | |
| H | PTR321 | |
| H | TYR449 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | TYR145 | |
| B | TYR145 | |
| C | TYR145 | |
| D | TYR145 | |
| E | TYR145 | |
| F | TYR145 | |
| G | TYR145 | |
| H | TYR145 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q63470 |
| Chain | Residue | Details |
| A | TYR219 | |
| B | TYR219 | |
| C | TYR219 | |
| D | TYR219 | |
| E | TYR219 | |
| F | TYR219 | |
| G | TYR219 | |
| H | TYR219 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23665168 |
| Chain | Residue | Details |
| A | SER310 | |
| B | SER310 | |
| C | SER310 | |
| D | SER310 | |
| E | SER310 | |
| F | SER310 | |
| G | SER310 | |
| H | SER310 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23665168 |
| Chain | Residue | Details |
| A | THR402 | |
| B | THR402 | |
| C | THR402 | |
| D | THR402 | |
| E | THR402 | |
| F | THR402 | |
| G | THR402 | |
| H | THR402 |
