1DEK
DEOXYNUCLEOSIDE MONOPHOSPHATE KINASE COMPLEXED WITH DEOXY-GMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004798 | molecular_function | dTMP kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006260 | biological_process | DNA replication |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0039693 | biological_process | viral DNA genome replication |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047507 | molecular_function | deoxynucleoside phosphate kinase activity, ATP as phosphate donor |
| A | 0050316 | molecular_function | dGMP kinase activity |
| A | 0052031 | biological_process | symbiont-mediated perturbation of host defense response |
| A | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
| A | 0099018 | biological_process | symbiont-mediated evasion of host restriction-modification system |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004798 | molecular_function | dTMP kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006260 | biological_process | DNA replication |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0039693 | biological_process | viral DNA genome replication |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047507 | molecular_function | deoxynucleoside phosphate kinase activity, ATP as phosphate donor |
| B | 0050316 | molecular_function | dGMP kinase activity |
| B | 0052031 | biological_process | symbiont-mediated perturbation of host defense response |
| B | 0052170 | biological_process | symbiont-mediated suppression of host innate immune response |
| B | 0099018 | biological_process | symbiont-mediated evasion of host restriction-modification system |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 300 |
| Chain | Residue |
| A | TYR42 |
| A | GLN85 |
| A | CYS88 |
| A | GLU108 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 300 |
| Chain | Residue |
| B | TYR42 |
| B | GLN85 |
| B | CYS88 |
| B | GLU108 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE DGP A 301 |
| Chain | Residue |
| A | ALA33 |
| A | LYS37 |
| A | ARG68 |
| A | ARG132 |
| A | MET135 |
| A | GLY139 |
| A | THR140 |
| A | VAL144 |
| A | TRP152 |
| A | ASP175 |
| A | ARG177 |
| A | GLN178 |
| A | GLU181 |
| A | THR208 |
| A | HOH304 |
| A | HOH305 |
| A | HOH325 |
| A | HOH346 |
| A | HOH364 |
| A | HOH424 |
| A | LYS10 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DGP B 301 |
| Chain | Residue |
| B | LEU32 |
| B | ALA33 |
| B | LYS37 |
| B | ARG68 |
| B | ARG132 |
| B | MET135 |
| B | THR140 |
| B | TRP152 |
| B | ASP175 |
| B | GLN178 |
| B | GLU181 |
| B | HOH317 |
| B | HOH342 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8670851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DEK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8670851","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1DEL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8670851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DEK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DEL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8670851","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DEL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 8670851 |
| Chain | Residue | Details |
| A | ARG68 | |
| A | HIS206 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 8670851 |
| Chain | Residue | Details |
| B | ARG68 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 637 |
| Chain | Residue | Details |
| A | ASP15 | |
| A | LEU72 | electrostatic stabiliser |
| A | ALA210 | electrostatic stabiliser, metal ligand |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 637 |
| Chain | Residue | Details |
| B | ASP15 | |
| B | LEU72 | electrostatic stabiliser |
| B | ALA210 | electrostatic stabiliser, metal ligand |
