Structure of PDB 5h63 Chain A Binding Site BS01

Receptor Information
>5h63 Chain A (length=309) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SGHVSFAGIDYPLLPLNHQTPLVFQWFERNPDRFGQNEIPIINTQKNPYL
NNIINAAIIEKERIIGIFVDGDFSKGQRKALGKLEQNYRNIKVIYNSDLN
YSMYDKKLTTIYLENITKLEAQSASERDEVLLNGVKKSLEDVLKNNPEET
LISSHNKDKGHLWFDFYRNLFLLKGSDAFLEAGKPGCHHLQPGGGCIYLD
ADMLLTDKLGTLYLPDGIAIHVSRKDNHVSLENGIIAVNRSEHPALIKGL
EIMHSKPYGDPYNDWLSKGLRHYFDGSHIQDYDAFCDFIEFKHENIIMNT
SSLTASSWR
Ligand information
Ligand IDUD1
InChIInChI=1S/C17H27N3O17P2/c1-6(22)18-10-13(26)11(24)7(4-21)35-16(10)36-39(31,32)37-38(29,30)33-5-8-12(25)14(27)15(34-8)20-3-2-9(23)19-17(20)28/h2-3,7-8,10-16,21,24-27H,4-5H2,1H3,(H,18,22)(H,29,30)(H,31,32)(H,19,23,28)/t7-,8-,10-,11-,12-,13-,14-,15-,16-/m1/s1
InChIKeyLFTYTUAZOPRMMI-CFRASDGPSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)NC1C(C(C(OC1OP(=O)(O)OP(=O)(O)OCC2C(C(C(O2)N3C=CC(=O)NC3=O)O)O)CO)O)O
CACTVS 3.341CC(=O)N[CH]1[CH](O)[CH](O)[CH](CO)O[CH]1O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O
ACDLabs 10.04O=P(OC1OC(C(O)C(O)C1NC(=O)C)CO)(O)OP(=O)(O)OCC3OC(N2C=CC(=O)NC2=O)C(O)C3O
CACTVS 3.341CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[P@](O)(=O)O[P@](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O
OpenEye OEToolkits 1.5.0CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]2[C@H]([C@H]([C@@H](O2)N3C=CC(=O)NC3=O)O)O)CO)O)O
FormulaC17 H27 N3 O17 P2
NameURIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
ChEMBLCHEMBL388154
DrugBankDB03397
ZINCZINC000008551100
PDB chain5h63 Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5h63 Structural basis for arginine glycosylation of host substrates by bacterial effector proteins.
Resolution1.92 Å
Binding residue
(original residue number in PDB)		Q64 W65 F66 Y88 H200 F203 D204 R207 D239 D241 N272 G273 N338 S340 S345 S346 W347 R348
Binding residue
(residue number reindexed from 1)		Q25 W26 F27 Y49 H161 F164 D165 R168 D200 D202 N233 G234 N299 S301 S306 S307 W308 R309
Annotation score3
Binding affinityPDBbind-CN: -logKd/Ki=5.92,Kd=1.2uM
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

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

[Back to BioLiP]