5FSL
MTH1 substrate recognition: Complex with a methylaminopurinone
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 | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 8 | 
| Details | BINDING SITE FOR RESIDUE UAN A 1157 | 
| Chain | Residue | 
| A | ASN33 | 
| A | PHE72 | 
| A | PHE74 | 
| A | TRP117 | 
| A | ASP119 | 
| A | ASP120 | 
| A | TRP123 | 
| A | HOH2019 | 
| site_id | AC2 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE SO4 A 1158 | 
| Chain | Residue | 
| A | ARG151 | 
| A | HOH2104 | 
| A | HIS134 | 
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 | 129 | 
| 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 | 21 | 
| 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 | 6 | 
| 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 | 1 | 
| 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 | 3 | 
| 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 | 5 | 
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q7ZWC3","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 











