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 | |
D | ILE165 | |
D | LYS188 | |
D | PHE238 | |
E | ILE165 | |
E | LYS188 | |
E | PHE238 | |
F | ILE165 | |
F | LYS188 | |
F | PHE238 | |
G | ILE165 | |
A | LYS188 | |
G | LYS188 | |
G | PHE238 | |
H | ILE165 | |
H | LYS188 | |
H | PHE238 | |
A | PHE238 | |
B | ILE165 | |
B | LYS188 | |
B | PHE238 | |
C | ILE165 | |
C | LYS188 | |
C | 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 | |
B | TYR319 | |
B | PTR321 | |
B | TYR449 | |
C | TYR140 | |
C | TYR159 | |
C | TYR177 | |
C | TYR319 | |
C | PTR321 | |
C | TYR449 | |
D | TYR140 | |
A | TYR159 | |
D | TYR159 | |
D | TYR177 | |
D | TYR319 | |
D | PTR321 | |
D | TYR449 | |
E | TYR140 | |
E | TYR159 | |
E | TYR177 | |
E | TYR319 | |
E | PTR321 | |
A | TYR177 | |
E | TYR449 | |
F | TYR140 | |
F | TYR159 | |
F | TYR177 | |
F | TYR319 | |
F | PTR321 | |
F | TYR449 | |
G | TYR140 | |
G | TYR159 | |
G | TYR177 | |
A | TYR319 | |
G | TYR319 | |
G | PTR321 | |
G | TYR449 | |
H | TYR140 | |
H | TYR159 | |
H | TYR177 | |
H | TYR319 | |
H | PTR321 | |
H | TYR449 | |
A | PTR321 | |
A | TYR449 | |
B | TYR140 | |
B | TYR159 | |
B | TYR177 |
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 |