Structure of PDB 2o3z Chain A

Receptor sequence
>2o3zA (length=267) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
GLEKTVKEKLSFEGVGIHTGEYSKLIIHPEKEGTGIRFFKNGVYIPARHE
FVVHTNHSTDLGFKGQRIKTVEHILSVLHLLEITNVTIEVIGNEIPILDG
SGWEFYEAIRKNILNQNREIDYFVVEEPIIVEDEGRLIKAEPSDTLEVTY
EGEFKNFLGRQKFTFVEGNEEEIVLARTFAFDWEIEHIKKVGLGKGGSLK
NTLVLGKDKVYNPEGLRYENEPVRHKVFDLIGDLYLLGSPVKGKFYSFRG
GHSLNVKLVKELAKKQK
3D structure
PDB2o3z Amphipathic benzoic acid derivatives: synthesis and binding in the hydrophobic tunnel of the zinc deacetylase LpxC.
ChainA
Resolution2.25 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 H79 H238 D242 H73 H225 D229
BS02 ZN A H58 H200 H57 H187
BS03 AI7 A I198 K202 G210 S211 I185 K189 G197 S198 MOAD: Kd=2uM
PDBbind-CN: -logKd/Ki=5.70,Kd=2uM
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:2o3z, PDBe:2o3z, PDBj:2o3z
PDBsum2o3z
PubMed17296300
UniProtO67648|LPXC_AQUAE UDP-3-O-acyl-N-acetylglucosamine deacetylase (Gene Name=lpxC)

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