Structure of PDB 2ves Chain C

Receptor sequence
>2vesC (length=299) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
MIKQRTLKNIIRATGVGLHSGEKVYLTLKPAPVDTGIVFSRTDLDPVVEI
PARAENVGETTMSTTLVKGDVKVDTVEHLLSAMAGLGIDNAYVELSASEV
PIMDGSAGPFVFLIQSAGLQEQEAAKKFIRIKREVSVEEGDKRAVFVPFD
GFKVSFEIDFDHPVFRGRTQQASVDFSSTSFVKEVSRARTFGFMRDIEYL
RSQNLALGGSVENAIVVDENRVLNEDGLRYEDEFVKHKILDAIGDLYLLG
NSLIGEFRGFKSGHALNNQLLRTLIADKDAWEVVTFEDARTAPISYMRP
3D structure
PDB2ves Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor.
ChainC
Resolution1.9 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 C H162 E219 H162 E219
BS02 ZN C H78 H237 D241 H78 H237 D241
BS03 GVR C L18 M62 E77 H78 T190 F191 G192 I197 G209 N213 A214 H237 D241 H264 L18 M62 E77 H78 T190 F191 G192 I197 G209 N213 A214 H237 D241 H264 PDBbind-CN: -logKd/Ki=7.70,Ki=20nM
BS04 ZN C D159 D161 D159 D161
BS05 ZN C E134 S136 E134 S136
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:2ves, PDBe:2ves, PDBj:2ves
PDBsum2ves
PubMed18287278
UniProtP47205|LPXC_PSEAE UDP-3-O-acyl-N-acetylglucosamine deacetylase (Gene Name=lpxC)

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