Structure of PDB 5dro Chain B

Receptor sequence
>5droB (length=267) Species: 224324 (Aquifex aeolicus VF5) [Search protein sequence]
GLEKTVKEKLSFEGVGIHTGEYSKLIIHPEKEGTGIRFFKNGVYIPARHE
FVVHTNHSTDLGFKGQRIKTVEHILSVLHLLEITNVTIEVIGNEIPILDG
SGWEFYEAIRKNILNQNREIDYFVVEEPIIVEDEGRLIKAEPSDTLEVTY
EGEFKNFLGRQKFTFVEGNEEEIVLARTFAFDWEIEHIKKVGLGKGGSLK
NTLVLGKDKVYNPEGLRYENEPVRHKVFDLIGDLYLLGSPVKGKFYSFRG
GHSLNVKLVKELAKKQK
3D structure
PDB5dro Drug design from the cryptic inhibitor envelope.
ChainB
Resolution2.01 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 B H74 H226 D230 H73 H225 D229
BS02 ZH2 B E73 H74 T179 A181 I189 G198 S199 T203 H226 D230 H253 E72 H73 T178 A180 I188 G197 S198 T202 H225 D229 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:5dro, PDBe:5dro, PDBj:5dro
PDBsum5dro
PubMed26912110
UniProtO67648|LPXC_AQUAE UDP-3-O-acyl-N-acetylglucosamine deacetylase (Gene Name=lpxC)

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