Structure of PDB 4oze Chain A

Receptor sequence
>4ozeA (length=266) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
GLEKTVKEKLSFEGVGIHTGEYSKLIIHPEKEGTGIRFFKNGVYIPARHE
FVVHTNHSTDLGFKGQRIKTVEHILSVLHLLEITNVTIEVIGNEIPILDG
SGWEFYEAIRKNILNQNREIDYFVVEEPIIVEDEGRLIKAEPSDTLEVTY
EGEFKNFLGRQKFTFVEGNEEEIVLARTFCFDWEIEHIKKVGLGKGGSLK
NTLVLGKDKVYNPEGLRYENEPVRHKVFDLIGDLYLLGSPVKGKFYSFRG
GHSLNVKLVKELAKKQ
3D structure
PDB4oze Mechanistic insight from the crystal structure of A.aolicus LpxC in the presence of product
ChainA
Resolution1.61 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 H74 H226 D230 H73 H225 D229
BS02 ZN A H58 H188 H57 H187
BS03 ZN A G2 E120 G1 E119
BS04 ZN A E73 H253 E72 H252
BS05 24G A H19 H58 R137 G153 E154 F155 F180 C181 E185 G195 G198 K227 R250 G252 H253 H18 H57 R136 G152 E153 F154 F179 C180 E184 G194 G197 K226 R249 G251 H252
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:4oze, PDBe:4oze, PDBj:4oze
PDBsum4oze
PubMed
UniProtO67648|LPXC_AQUAE UDP-3-O-acyl-N-acetylglucosamine deacetylase (Gene Name=lpxC)

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