Structure of PDB 6p89 Chain A

Receptor sequence
>6p89A (length=335) Species: 562 (Escherichia coli) [Search protein sequence]
SIRLADLAQQLDAELHGDGDIVITGVASMQSAQTGHITFMVNPKYREHLG
LCQASAVVMTQDDLPFAKSAALVVKNPYLTYARMAQILDTTPQPAQNIAP
SAVIDATAKLGNNVSIGANAVIESGVELGDNVIIGAGCFVGKNSKIGAGS
RLWANVTIYHEIQIGQNCLIQSGTVVGADGFGYANDRGNWVKIPQIGRVI
IGDRVEIGACTTIDRGALDDTIIGNGVIIDNQCQIAHNVVIGDNTAVAGG
VIMAGSLKIGRYCMIGGASVINGHMEICDKVTVTGMGMVMRPITEPGVYS
SGIPLQPNKVWRKTAALVMNIDDMSKRLKSLERKV
3D structure
PDB6p89 Structural and Biological Basis of Small Molecule Inhibition ofEscherichia coliLpxD Acyltransferase Essential for Lipopolysaccharide Biosynthesis.
ChainA
Resolution1.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.191: UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase.
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 O4A A M266 I267 G268 T286 G287 M264 I265 G266 T284 G285 PDBbind-CN: -logKd/Ki=5.01,Kd=9.77uM
BS02 O3V A F183 I254 A256 F181 I252 A254
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016410 N-acyltransferase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0042802 identical protein binding
GO:0103118 UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase activity
Biological Process
GO:0009245 lipid A biosynthetic process
GO:0046677 response to antibiotic
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6p89, PDBe:6p89, PDBj:6p89
PDBsum6p89
PubMed31402665
UniProtP21645|LPXD_ECOLI UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (Gene Name=lpxD)

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