Structure of PDB 5h60 Chain A Binding Site BS02

Receptor Information
>5h60 Chain A (length=304) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SFNGKDYPLCFLDEKTPLLFQWFERNPARFGKNDIPIINTEKNPYLNNII
KAATIEKERLIGIFVDGDFFPGQKDAFSKLEYDYENIKVIYRNDIDFSMY
DKKLSEIYMENISKQESMPEEKRDCHLLQLLKKELSDIQEGNDSLIKSYL
LDKGHGWFDFYRNMAMLKAGQLFLEADKVGCYDLSTNSGCIYLDADMIIT
EKLGGIYIPDGIAVHVERIDGRASMENGIIAVDRNNHPALLAGLEIMHTK
FDADPYSDGVCNGIRKHFNYSLNEDYNSFCDFIEFKHDNIIMNTSQFTQS
SWAR
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 chain5h60 Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5h60 Structural basis for arginine glycosylation of host substrates by bacterial effector proteins.
Resolution3.64 Å
Binding residue
(original residue number in PDB)		D225 N322 S324
Binding residue
(residue number reindexed from 1)		D196 N293 S295
Annotation score1
Enzymatic activity
Enzyme Commision number 2.4.1.-
Gene Ontology
Molecular Function
GO:0016757 glycosyltransferase activity
GO:0046872 metal ion binding
GO:0090729 toxin activity
GO:0106362 protein-arginine N-acetylglucosaminyltransferase activity
Biological Process
GO:0035821 modulation of process of another organism
Cellular Component
GO:0005576 extracellular region
GO:0030430 host cell cytoplasm
GO:0044164 host cell cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5h60, PDBe:5h60, PDBj:5h60
PDBsum5h60
PubMed30327479
UniProtQ9L9J3|SSEK1_SALTY Protein-arginine N-acetylglucosaminyltransferase SseK1 (Gene Name=sseK1)

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