Structure of PDB 6moo Chain A

Receptor sequence
>6mooA (length=301) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
HHEGAGTIKQRTLKNIIRATGVGLHSGEKVYLTLKPAPVDTGIVFSRTDL
DPVVEIPARAENVGETTMSTTLVKGDVKVDTVEHLLSAMAGLGIDNAYVE
LSASEVPIMDGSAGPFVFLIQSAGLQEQEAAKKFIRIKREVSVEEGDKRA
VFVPFDGFKVSFEIDFDHPVFQQASVDFSSTSFVKEVSRARTFGFMRDIE
YLRSQNLALGGSVENAIVVDENRVLNEDGLRYEDEFVKHKILDAIGDLYL
LGNSLIGEFRGFKSGHALNNQLLRTLIADKDAWEVVTFEDARTAPISYMR
P
3D structure
PDB6moo Optimization of LpxC Inhibitors for Antibacterial Activity and Cardiovascular Safety.
ChainA
Resolution2.2 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 H84 H239 D243
BS02 A5F A E77 T190 F191 I197 G209 S210 H237 D241 H264 E83 T192 F193 I199 G211 S212 H239 D243 H266 MOAD: ic50=19nM
PDBbind-CN: -logKd/Ki=9.17,IC50=0.68nM
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:6moo, PDBe:6moo, PDBj:6moo
PDBsum6moo
PubMed31283109
UniProtP47205|LPXC_PSEAE UDP-3-O-acyl-N-acetylglucosamine deacetylase (Gene Name=lpxC)

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