Structure of PDB 7x9h Chain A

Receptor sequence
>7x9hA (length=129) Species: 562 (Escherichia coli) [Search protein sequence]
MKKLQIAVGIIRNENNEIFITRRAADAHMANKLEFPGGKIEMGETPEQAV
VRELQEEVGITPQHFSLFEKLEYEFPDRHITLWFWLVERWEGEPWGKEGQ
PGEWMSLVGLNADDFPPANEPVIAKLKRL
3D structure
PDB7x9h Visualization of mutagenic nucleotide processing by Escherichia coli MutT, a Nudix hydrolase.
ChainA
Resolution1.69 Å
3D
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Enzymatic activity
Enzyme Commision number 3.6.1.55: 8-oxo-dGTP 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 GLC A H64 F65 H64 F65
BS02 8DG A I6 V8 R23 H28 E34 F35 G37 G38 I80 L82 P116 N119 I6 V8 R23 H28 E34 F35 G37 G38 I80 L82 P116 N119
BS03 8OG A I6 V8 R23 H28 E34 F35 G37 I80 L82 P116 N119 I6 V8 R23 H28 E34 F35 G37 I80 L82 P116 N119
BS04 MN A G37 E57 G37 E57
BS05 MN A E53 E57 E53 E57
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005515 protein binding
GO:0008413 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
GO:0016787 hydrolase activity
GO:0030145 manganese ion binding
GO:0035539 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity
GO:0044715 8-oxo-dGDP phosphatase activity
GO:0044716 8-oxo-GDP phosphatase activity
GO:0046872 metal ion binding
GO:0047693 ATP diphosphatase activity
Biological Process
GO:0006203 dGTP catabolic process
GO:0006260 DNA replication
GO:0006281 DNA repair
GO:0006289 nucleotide-excision repair
GO:0046067 dGDP catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7x9h, PDBe:7x9h, PDBj:7x9h
PDBsum7x9h
PubMed35594391
UniProtP08337|MUTT_ECOLI 8-oxo-dGTP diphosphatase (Gene Name=mutT)

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