Structure of PDB 7x9h Chain A Binding Site BS05

Receptor Information
>7x9h Chain A (length=129) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKKLQIAVGIIRNENNEIFITRRAADAHMANKLEFPGGKIEMGETPEQAV
VRELQEEVGITPQHFSLFEKLEYEFPDRHITLWFWLVERWEGEPWGKEGQ
PGEWMSLVGLNADDFPPANEPVIAKLKRL
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain7x9h Chain A Residue 206 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7x9h Visualization of mutagenic nucleotide processing by Escherichia coli MutT, a Nudix hydrolase.
Resolution1.69 Å
Binding residue
(original residue number in PDB)		E53 E57
Binding residue
(residue number reindexed from 1)		E53 E57
Annotation score1
Enzymatic activity
Enzyme Commision number 3.6.1.55: 8-oxo-dGTP diphosphatase.
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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