5HZX
Crystal structure of zebrafish MTH1 in complex with TH588
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0008413 | molecular_function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity |
| A | 0008828 | molecular_function | dATP diphosphatase activity |
| A | 0009151 | biological_process | purine deoxyribonucleotide metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| A | 0042262 | biological_process | DNA protection |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047429 | molecular_function | nucleoside triphosphate diphosphatase activity |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0008413 | molecular_function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity |
| B | 0008828 | molecular_function | dATP diphosphatase activity |
| B | 0009151 | biological_process | purine deoxyribonucleotide metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| B | 0042262 | biological_process | DNA protection |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047429 | molecular_function | nucleoside triphosphate diphosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue 2GE A 201 |
| Chain | Residue |
| A | THR8 |
| A | ASN33 |
| A | PHE72 |
| A | PHE74 |
| A | MET81 |
| A | TRP117 |
| A | ASP119 |
| A | ASP120 |
| A | SO4202 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 202 |
| Chain | Residue |
| A | LEU9 |
| A | LYS23 |
| A | ASN33 |
| A | GLY34 |
| A | GLY36 |
| A | GLY37 |
| A | GLU56 |
| A | 2GE201 |
| A | HOH339 |
| B | LEU156 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 203 |
| Chain | Residue |
| A | ARG132 |
| A | HOH311 |
| A | HOH347 |
| B | ARG25 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 204 |
| Chain | Residue |
| A | ASP62 |
| A | THR63 |
| A | HIS65 |
| A | ASP89 |
| A | ASN90 |
| A | HOH308 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 205 |
| Chain | Residue |
| A | ASN90 |
| A | TYR91 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PEG A 206 |
| Chain | Residue |
| A | GLU46 |
| A | GLN47 |
| A | ARG50 |
| A | GLN115 |
| A | HOH310 |
| A | HOH324 |
| A | HOH340 |
| A | HOH356 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue 2GE B 201 |
| Chain | Residue |
| B | THR8 |
| B | PHE27 |
| B | ASN33 |
| B | PHE72 |
| B | MET81 |
| B | TRP117 |
| B | ASP119 |
| B | ASP120 |
| B | SO4202 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 202 |
| Chain | Residue |
| A | LEU156 |
| B | LYS23 |
| B | GLY34 |
| B | GLY36 |
| B | GLY37 |
| B | GLU56 |
| B | 2GE201 |
| B | HOH324 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 203 |
| Chain | Residue |
| A | ARG25 |
| B | ARG132 |
| B | HOH334 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 204 |
| Chain | Residue |
| A | HOH335 |
| B | LEU122 |
| B | HOH309 |
| B | HOH347 |
Functional Information from PROSITE/UniProt
| site_id | PS00893 |
| Number of Residues | 22 |
| Details | NUDIX_BOX Nudix box signature. GkvqtgEtieqAArRELlEEsG |
| Chain | Residue | Details |
| A | GLY37-GLY58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 258 |
| Details | Domain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 42 |
| Details | Motif: {"description":"Nudix box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30304478","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OTN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
