6GLJ
Crystal structure of hMTH1 F27A in complex with TH scaffold 1 in the absence of acetate
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 | 3 |
Details | binding site for residue SO4 A 201 |
Chain | Residue |
A | HIS134 |
A | ARG151 |
A | HOH349 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue SO4 A 202 |
Chain | Residue |
A | HOH305 |
A | HOH332 |
A | HOH386 |
A | HOH410 |
A | PRO95 |
A | TRP105 |
A | ARG151 |
A | VAL153 |
A | ASP154 |
A | THR155 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 203 |
Chain | Residue |
A | HIS65 |
A | LYS66 |
A | HOH314 |
A | HOH335 |
A | HOH387 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 204 |
Chain | Residue |
A | LYS138 |
A | LYS138 |
A | ASP147 |
A | ASP147 |
A | HOH325 |
A | HOH325 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue F3E A 205 |
Chain | Residue |
A | TYR7 |
A | ASN33 |
A | PHE72 |
A | TRP117 |
A | ASP119 |
A | ASP120 |
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 |