Structure of PDB 5h63 Chain C Binding Site BS03

Receptor Information
>5h63 Chain C (length=302) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GHVSFAGIDYPLLPLNHQTPLVFQWFERNPDRFGQNEIPIINTQKNPYLN
NIINAAIIEKERIIGIFVDGDFSKGQRKALGKLEQNYRNIKVIYNSDLNY
SMYDKKLTTIYLENITKLEAQSASERDEVLLNGVKKSLEDVLKNNPEETL
ISSHNKDKGHLWFDFYRNLFLLKGSDAFLEAGKPGCHHLQPGGGCIYLDA
DMLLTDKLGTLYLPDGIAIHVSRKDNHVSLENGIIAVNRSEHPALIKGLE
IMHSKPYGDPYNDWLSKGLRHYFDGSHIQDYDAFCDFIEFKHENIIMNTS
SL
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 chain5h63 Chain C Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5h63 Structural basis for arginine glycosylation of host substrates by bacterial effector proteins.
Resolution1.92 Å
Binding residue
(original residue number in PDB)		D241 N338 S340
Binding residue
(residue number reindexed from 1)		D201 N298 S300
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:0043657 host cell
GO:0044177 host cell Golgi apparatus

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5h63, PDBe:5h63, PDBj:5h63
PDBsum5h63
PubMed30327479
UniProtQ8ZNP4|SSEK2_SALTY Protein-arginine N-acetylglucosaminyltransferase SseK2 (Gene Name=sseK2)

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