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5FSK

MTH1 substrate recognition: Complex with 8-oxo-dGTP.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001669cellular_componentacrosomal vesicle
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006152biological_processpurine nucleoside catabolic process
A0006281biological_processDNA repair
A0006979biological_processresponse to oxidative stress
A0008413molecular_function8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
A0008584biological_processmale gonad development
A0008828molecular_functiondATP diphosphatase activity
A0016787molecular_functionhydrolase activity
A0016818molecular_functionhydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
A0030515molecular_functionsnoRNA binding
A0031965cellular_componentnuclear membrane
A0035539molecular_function8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity
A0042262biological_processDNA protection
A0046686biological_processresponse to cadmium ion
A0046872molecular_functionmetal ion binding
A0047693molecular_functionATP diphosphatase activity
A0106377molecular_function2-hydroxy-ATP hydrolase activity
A0106378molecular_function2-hydroxy-dATP hydrolase activity
A0106431molecular_functionN6-methyl-(d)ATP hydrolase activity
A0106433molecular_functionO6-methyl-dGTP hydrolase activity
A0140933molecular_function5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE H6Y A 1157
ChainResidue
ATYR7
AMET81
ATRP117
AASP119
AASP120
AACT1158
AHOH2013
AHOH2018
AHOH2023
AHOH2034
AHOH2074
APHE27
AASN33
AGLY36
AGLY37
ALYS38
AGLU52
AGLU56
APHE72

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 1158
ChainResidue
ALEU9
AASN33
AGLY34
AASP120
ATRP123
APHE124
AH6Y1157

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GkvqegEtiedGArRELqEEsG
ChainResidueDetails
AGLY37-GLY58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q7ZWC3
ChainResidueDetails
ALEU11
AGLN14
APRO15
ALEU59

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:30304478, ECO:0007744|PDB:5OTM
ChainResidueDetails
AGLY76

218853

PDB entries from 2024-04-24

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