Structure of PDB 2ier Chain A

Receptor sequence
>2ierA (length=267) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
GLEKTVKEKLSFEGVGIHTGEYSKLIIHPEKEGTGIRFFKNGVYIPARHE
FVVHTNHSTDLGFKGQRIKTVEHILSVLHLLEITNVTIEVIGNEIPILDG
SGWEFYEAIRKNILNQNREIDYFVVEEPIIVEDEGRLIKAEPSDTLEVTY
EGEFKNFLGRQKFTFVEGNEEEIVLARTFAFDWEIEHIKKVGLGKGGSLK
NTLVLGKDKVYNPEGLRYENEPVRHKVFDLIGDLYLLGSPVKGKFYSFRG
GHSLNVKLVKELAKKQK
3D structure
PDB2ier Binding of Uridine 5-Diphosphate in the Basic Patch of the Zinc Metalloenzyme Deacetylase LpxC and Implications for Substrate Binding
ChainA
Resolution2.7 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 ZN A G2 E126 G1 E119
BS04 ZN A E78 H265 E72 H252
BS05 UDP A H58 G159 E160 F161 F194 E197 K239 R262 H265 H57 G152 E153 F154 F181 E184 K226 R249 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
View graph for
Biological Process
External links
PDB RCSB:2ier, PDBe:2ier, PDBj:2ier
PDBsum2ier
PubMed17176043
UniProtO67648|LPXC_AQUAE UDP-3-O-acyl-N-acetylglucosamine deacetylase (Gene Name=lpxC)

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