Structure of PDB 5drq Chain A

Receptor sequence
>5drqA (length=296) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
MIKQRTLKNIIRATGVGLHSGEKVYLTLKPAPVDTGIVFSRTDLDPVVEI
PARAENVGETTMSTTLVKGDVKVDTVEHLLSAMAGLGIDNAYVELSASEV
PIMDGSAGPFVFLIQSAGLQEQEAAKKFIRIKREVSVEEGDKRAVFVPFD
GFKVSFEIDFDHPVFRGRTQQASVDFSSTSFVKEVSRARTFGFMRDIEYL
RSQNLALGGSVENAIVVDENRVLNEDGLRYEDEFVKHKILDAIGDLYLLG
NSLIGEFRGFKSGHALNNQLLRTLIADKDAWEVVTFEDARTAPISY
3D structure
PDB5drq Drug design from the cryptic inhibitor envelope.
ChainA
Resolution1.63 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 A H78 H237 D241 H78 H237 D241
BS02 ZN A H162 E219 H162 E219
BS03 5EM A E77 T190 F191 I197 R201 G209 S210 H237 D241 H264 E77 T190 F191 I197 R201 G209 S210 H237 D241 H264 PDBbind-CN: -logKd/Ki=10.92,Ki=12pM
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:5drq, PDBe:5drq, PDBj:5drq
PDBsum5drq
PubMed26912110
UniProtP47205|LPXC_PSEAE UDP-3-O-acyl-N-acetylglucosamine deacetylase (Gene Name=lpxC)

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