Structure of PDB 6i49 Chain BBB

Receptor sequence
>6i49BBB (length=298) Species: 557722 (Pseudomonas aeruginosa LESB58) [Search protein sequence]
MIKQRTLKNIIRATGVGLHSGEKVYLTLKPAPVDTGIVFSRTDLDPVVEI
PARAENVGETTMSTTLVKGDVKVDTVEHLLSAMAGLGIDNAYVELSASEV
PIMDGSAGPFVFLIQSAGLQEQEAAKKFIRIKREVSVEEGDKRAVFVPFD
GFKVSFEIDFDHPVFRGRTQQASVDFSSTSFVKEVSRARTFGFMRDIEYL
RSQNLALGGSVENAIVVDENRVLNEDGLRYEDEFVKHKILDAIGDLYLLG
NSLIGEFRGFKSGHALNNQLLRTLIADKDAWEVVTFEDARTAPISYMR
3D structure
PDB6i49 Discovery of Novel Inhibitors of LpxC Displaying Potent in Vitro Activity against Gram-Negative Bacteria.
ChainBBB
Resolution1.94 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.108: UDP-3-O-acyl-N-acetylglucosamine deacetylase.
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 ZN BBB H78 H237 D241 H78 H237 D241
BS02 H2Z BBB L18 H19 M62 E77 T190 F191 A206 G209 H237 K238 D241 H264 L18 H19 M62 E77 T190 F191 A206 G209 H237 K238 D241 H264
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0103117 UDP-3-O-acyl-N-acetylglucosamine deacetylase activity
Biological Process
GO:0006796 phosphate-containing compound metabolic process
GO:0009245 lipid A biosynthetic process
GO:0019637 organophosphate metabolic process
GO:1901135 carbohydrate derivative metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6i49, PDBe:6i49, PDBj:6i49
PDBsum6i49
PubMed31804826
UniProtB7UZI4|LPXC_PSEA8 UDP-3-O-acyl-N-acetylglucosamine deacetylase (Gene Name=lpxC)

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