5FSM
MTH1 substrate recognition: Complex with a methylbenzimidazolyl acetamide.
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 | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 201 |
| Chain | Residue |
| A | PRO95 |
| A | ASP154 |
| A | HOH339 |
| A | HOH343 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE N91 A 202 |
| Chain | Residue |
| A | ASP119 |
| A | ASP120 |
| A | TRP123 |
| A | PHE124 |
| A | LEU9 |
| A | ASN33 |
| A | GLY34 |
| A | PHE72 |
| A | TRP117 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 203 |
| Chain | Residue |
| A | THR8 |
| A | GLY37 |
| A | HOH449 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 204 |
| Chain | Residue |
| A | TYR148 |
| A | THR149 |
| A | LEU150 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS A 205 |
| Chain | Residue |
| A | HIS65 |
| A | LYS66 |
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 | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q7ZWC3 |
| Chain | Residue | Details |
| A | LEU11 | |
| A | GLN14 | |
| A | PRO15 | |
| A | LEU59 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30304478, ECO:0007744|PDB:5OTM |
| Chain | Residue | Details |
| A | GLY76 |
