4N1U
Structure of human MTH1 in complex with TH588
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006152 | biological_process | purine nucleoside catabolic process |
| A | 0006281 | biological_process | DNA repair |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0008413 | molecular_function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity |
| A | 0008828 | molecular_function | dATP diphosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| A | 0030515 | molecular_function | snoRNA binding |
| A | 0035539 | molecular_function | 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity |
| A | 0042262 | biological_process | DNA protection |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047693 | molecular_function | ATP diphosphatase activity |
| A | 0106377 | molecular_function | 2-hydroxy-ATP hydrolase activity |
| A | 0106378 | molecular_function | 2-hydroxy-dATP hydrolase activity |
| A | 0106431 | molecular_function | N6-methyl-(d)ATP hydrolase activity |
| A | 0106433 | molecular_function | O6-methyl-dGTP hydrolase activity |
| A | 0140933 | molecular_function | 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006152 | biological_process | purine nucleoside catabolic process |
| B | 0006281 | biological_process | DNA repair |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0008413 | molecular_function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity |
| B | 0008828 | molecular_function | dATP diphosphatase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016818 | molecular_function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides |
| B | 0030515 | molecular_function | snoRNA binding |
| B | 0035539 | molecular_function | 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity |
| B | 0042262 | biological_process | DNA protection |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047693 | molecular_function | ATP diphosphatase activity |
| B | 0106377 | molecular_function | 2-hydroxy-ATP hydrolase activity |
| B | 0106378 | molecular_function | 2-hydroxy-dATP hydrolase activity |
| B | 0106431 | molecular_function | N6-methyl-(d)ATP hydrolase activity |
| B | 0106433 | molecular_function | O6-methyl-dGTP hydrolase activity |
| B | 0140933 | molecular_function | 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase 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 | PHE27 |
| A | ASN33 |
| A | PHE72 |
| A | TRP117 |
| A | ASP119 |
| A | ASP120 |
| A | TRP123 |
| A | PHE139 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 202 |
| Chain | Residue |
| A | LEU9 |
| A | LYS23 |
| A | GLY34 |
| A | GLY36 |
| A | GLU56 |
| A | MET101 |
| A | HOH304 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 203 |
| Chain | Residue |
| A | GLU77 |
| B | HIS65 |
| B | LYS66 |
| B | LYS132 |
| B | SO4204 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 204 |
| Chain | Residue |
| A | TYR122 |
| A | TYR148 |
| A | HOH335 |
| B | LYS24 |
| B | TYR136 |
| B | LYS138 |
| B | SO4203 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 205 |
| Chain | Residue |
| A | ALA63 |
| A | HIS65 |
| A | THR88 |
| A | ASP89 |
| A | SER90 |
| A | HOH354 |
| B | GLN142 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 206 |
| Chain | Residue |
| A | LYS23 |
| A | GLY26 |
| A | PHE27 |
| B | LYS114 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 207 |
| Chain | Residue |
| A | LYS66 |
| A | HIS134 |
| B | ARG17 |
| B | HOH330 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 208 |
| Chain | Residue |
| A | PHE113 |
| A | SER121 |
| A | PRO125 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 2GE B 201 |
| Chain | Residue |
| B | TYR7 |
| B | THR8 |
| B | PHE27 |
| B | ASN33 |
| B | PHE72 |
| B | PHE74 |
| B | MET81 |
| B | TRP117 |
| B | ASP119 |
| B | ASP120 |
| B | TRP123 |
| B | PHE139 |
| B | SO4202 |
| B | HOH369 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 202 |
| Chain | Residue |
| B | LYS23 |
| B | ASN33 |
| B | GLY34 |
| B | GLY36 |
| B | GLU56 |
| B | GLU100 |
| B | MET101 |
| B | 2GE201 |
| B | HOH307 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 203 |
| Chain | Residue |
| A | TYR122 |
| A | ILE145 |
| A | SO4204 |
| B | LYS24 |
| B | GLU97 |
| B | SER98 |
| B | ASP99 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 204 |
| Chain | Residue |
| A | PHE27 |
| A | PHE74 |
| A | GLU77 |
| A | GLY141 |
| A | GLN142 |
| A | SO4203 |
| B | HIS65 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 205 |
| Chain | Residue |
| A | SER121 |
| A | TYR122 |
| B | ARG25 |
| B | ASP99 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 206 |
| Chain | Residue |
| A | GLN142 |
| B | ALA63 |
| B | HIS65 |
| B | THR88 |
| B | ASP89 |
| B | SER90 |
| B | HOH352 |
| B | HOH401 |
Functional Information from PROSITE/UniProt
| site_id | PS00893 |
| Number of Residues | 22 |
| Details | NUDIX_BOX Nudix box signature. GkvqegEtiedGArRELqEEsG |
| 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 | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30304478","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OTM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26999531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FSK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26999531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28035004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FSI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5GHI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5GHM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q7ZWC3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
