Structure of PDB 7phj Chain A

Receptor sequence
>7phjA (length=299) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
IKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFP
ADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEI
PIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPYN
GFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEYL
QSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCG
HNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAP
3D structure
PDB7phj LpxC Inhibitors With Fluoroproline As A Novel Zinc-Binding Group Can Serve As A Novel Class of Antibiotic With Activity Against Multidrug-Resistant Gram-Negative Bacteria
ChainA
Resolution2.45 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 H78 H237 D241
BS02 7PX A L18 L62 E78 H79 T191 F192 F194 I198 C207 G210 S211 F212 H238 D242 H265 L17 L61 E77 H78 T190 F191 F193 I197 C206 G209 S210 F211 H237 D241 H264
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0019213 deacetylase 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
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7phj, PDBe:7phj, PDBj:7phj
PDBsum7phj
PubMed
UniProtP0A725|LPXC_ECOLI UDP-3-O-acyl-N-acetylglucosamine deacetylase (Gene Name=lpxC)

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