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1PUQ

Solution Structure of the MutT Pyrophosphohydrolase Complexed with Mg(2+) and 8-oxo-dGMP, a Tightly-bound Product

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0006203biological_processdGTP catabolic process
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006289biological_processnucleotide-excision repair
A0008413molecular_function8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0035539molecular_function8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity
A0044715molecular_function8-oxo-dGDP phosphatase activity
A0044716molecular_function8-oxo-GDP phosphatase activity
A0046067biological_processdGDP catabolic process
A0046872molecular_functionmetal ion binding
A0047693molecular_functionATP diphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 130
ChainResidue
AGLY38
ALYS39
AGLU53
AGLU56
AGLU57
AHOH5011
AHOH5012

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 8OG A 131
ChainResidue
AGLU34
APHE75
AARG78
AILE80
AALA118
AASN119
ALEU4
AILE6

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GkiemgEtpeqAVvRELqEEvG
ChainResidueDetails
AGLY38-GLY59

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:19864691
ChainResidueDetails
AARG23
AHIS28
AGLU34

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19864691
ChainResidueDetails
AGLY37
AGLU57

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:12939141, ECO:0000305|PubMed:19864691
ChainResidueDetails
AASN119

219140

PDB entries from 2024-05-01

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