Structure of PDB 8v24 Chain D

Receptor sequence
>8v24D (length=302) Species: 199310 (Escherichia coli CFT073) [Search protein sequence]
MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDF
PADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPE
IPIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPY
NGFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEY
LQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMC
GHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAP
SA
3D structure
PDB8v24 Dual function of LapB (YciM) in regulating Escherichia coli lipopolysaccharide synthesis.
ChainD
Resolution3.6 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 24G D L62 F161 F192 F194 I198 C207 G210 S211 A215 V217 K239 K262 L62 F161 F192 F194 I198 C207 G210 S211 A215 V217 K239 K262
BS02 ZN D E78 H79 H238 D242 E78 H79 H238 D242
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:8v24, PDBe:8v24, PDBj:8v24
PDBsum8v24
PubMed38635633
UniProtP0A726|LPXC_ECOL6 UDP-3-O-acyl-N-acetylglucosamine deacetylase (Gene Name=lpxC)

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