Structure of PDB 5lpg Chain A

Receptor sequence
>5lpgA (length=156) Species: 9606 (Homo sapiens) [Search protein sequence]
GRRPGVGVGVVVTSCKHPRCVLLGKRKGSVGAGSFQLPGGHLEFGETWEE
CAQRETWEEAALHLKNVHFASVVNSFIEKENYHYVTILMKGEVDVTHDSE
PKNVEPEKNESWEWVPWEELPPLDQLFWGLRCLKEQGYDPFKEDLNHLVG
YKGNHL
3D structure
PDB5lpg NUDT15 Hydrolyzes 6-Thio-DeoxyGTP to Mediate the Anticancer Efficacy of 6-Thioguanine.
ChainA
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.1.9: nucleotide diphosphatase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 MG A E63 E67 E55 E59
BS02 71V A Q44 L45 G47 G48 H49 Y90 F135 G137 L138 Q36 L37 G39 G40 H41 Y82 F127 G129 L130
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008413 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
GO:0016787 hydrolase activity
GO:0035539 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity
GO:0044715 8-oxo-dGDP phosphatase activity
GO:0046872 metal ion binding
GO:0047429 nucleoside triphosphate diphosphatase activity
Biological Process
GO:0000278 mitotic cell cycle
GO:0000302 response to reactive oxygen species
GO:0006195 purine nucleotide catabolic process
GO:0006203 dGTP catabolic process
GO:0009217 purine deoxyribonucleoside triphosphate catabolic process
GO:0042178 xenobiotic catabolic process
GO:0042262 DNA protection
GO:0055086 nucleobase-containing small molecule metabolic process
GO:0061136 regulation of proteasomal protein catabolic process
GO:1901292 nucleoside phosphate catabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5lpg, PDBe:5lpg, PDBj:5lpg
PDBsum5lpg
PubMed27530327
UniProtQ9NV35|NUD15_HUMAN Nucleotide triphosphate diphosphatase NUDT15 (Gene Name=NUDT15)

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