1P61
Structure of human dCK complexed with 2'-Deoxycytidine and ADP, P 43 21 2 space group
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0004136 | molecular_function | deoxyadenosine kinase activity |
B | 0004137 | molecular_function | deoxycytidine kinase activity |
B | 0004138 | molecular_function | deoxyguanosine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005829 | cellular_component | cytosol |
B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0006220 | biological_process | pyrimidine nucleotide metabolic process |
B | 0008144 | molecular_function | obsolete drug binding |
B | 0009224 | biological_process | CMP biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
B | 0019136 | molecular_function | deoxynucleoside kinase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0043771 | molecular_function | cytidine kinase activity |
B | 0106383 | biological_process | dAMP salvage |
B | 1901135 | biological_process | carbohydrate derivative metabolic process |
B | 1901293 | biological_process | nucleoside phosphate biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ADP B 301 |
Chain | Residue |
B | ALA31 |
B | GLU213 |
B | HIS218 |
B | VAL238 |
B | GLU240 |
B | ASP241 |
B | PHE242 |
B | HOH310 |
B | HOH311 |
B | HOH325 |
B | HOH326 |
B | ALA32 |
B | HOH341 |
B | HOH346 |
B | GLY33 |
B | LYS34 |
B | SER35 |
B | THR36 |
B | ARG188 |
B | ARG192 |
B | TYR210 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE DCZ B 302 |
Chain | Residue |
B | ILE30 |
B | GLU53 |
B | VAL55 |
B | TRP58 |
B | LEU82 |
B | MET85 |
B | TYR86 |
B | PHE96 |
B | GLN97 |
B | ARG128 |
B | ASP133 |
B | PHE137 |
B | GLU197 |
B | HOH303 |
B | HOH323 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255 |
Chain | Residue | Details |
B | GLU127 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: |
Chain | Residue | Details |
B | GLU53 | |
B | TYR86 | |
B | GLN97 | |
B | ARG128 | |
B | ASP133 | |
B | ARG188 | |
B | GLU197 | |
B | GLU240 | |
B | GLY28 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by CK1 => ECO:0000305|PubMed:20637175 |
Chain | Residue | Details |
B | SER11 | |
B | SER15 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by CK1 => ECO:0000305|PubMed:20637175 |
Chain | Residue | Details |
B | THR72 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:20637175, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER74 |