Structure of PDB 5h63 Chain A

Receptor sequence
>5h63A (length=309) Species: 562 (Escherichia coli) [Search protein sequence]
SGHVSFAGIDYPLLPLNHQTPLVFQWFERNPDRFGQNEIPIINTQKNPYL
NNIINAAIIEKERIIGIFVDGDFSKGQRKALGKLEQNYRNIKVIYNSDLN
YSMYDKKLTTIYLENITKLEAQSASERDEVLLNGVKKSLEDVLKNNPEET
LISSHNKDKGHLWFDFYRNLFLLKGSDAFLEAGKPGCHHLQPGGGCIYLD
ADMLLTDKLGTLYLPDGIAIHVSRKDNHVSLENGIIAVNRSEHPALIKGL
EIMHSKPYGDPYNDWLSKGLRHYFDGSHIQDYDAFCDFIEFKHENIIMNT
SSLTASSWR
3D structure
PDB5h63 Structural basis for arginine glycosylation of host substrates by bacterial effector proteins.
ChainA
Resolution1.92 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.4.1.-
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 UD1 A Q64 W65 F66 Y88 H200 F203 D204 R207 D239 D241 N272 G273 N338 S340 S345 S346 W347 R348 Q25 W26 F27 Y49 H161 F164 D165 R168 D200 D202 N233 G234 N299 S301 S306 S307 W308 R309 PDBbind-CN: -logKd/Ki=5.92,Kd=1.2uM
BS02 MN A D241 N338 S340 D202 N299 S301
BS03 MN A D322 D326 D283 D287
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]