Structure of PDB 4ihg Chain E Binding Site BS01
Receptor Information
>4ihg Chain E (length=337) Species:
83333
(Escherichia coli K-12) [
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ASIRLADLAQQLDAELHGDGDIVITGVASMQSAQTGHITFMVNPKYREHL
GLCQASAVVMTQDDLPFAKSAALVVKNPYLTYARMAQILDTTPQPAQNIA
PSAVIDATAKLGNNVSIGANAVIESGVELGDNVIIGAGCFVGKNSKIGAG
SRLWANVTIYHEIQIGQNCLIQSGTVVGADGFGYANDRGNWVKIPQIGRV
IIGDRVEIGACTTIDRGALDDTIIGNGVIIDNQCQIAHNVVIGDNTAVAG
GVIMAGSLKIGRYCMIGGASVINGHMEICDKVTVTGMGMVMRPITEPGVY
SSGIPLQPNKVWRKTAALVMNIDDMSKRLKSLERKVN
Ligand information
>4ihg Chain L (length=10) Species:
885275
(Escherichia coli str. 'clone D i14') [
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DSLDTVELVM
Receptor-Ligand Complex Structure
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PDB
4ihg
Chasing acyl carrier protein through a catalytic cycle of lipid A production.
Resolution
2.89 Å
Binding residue
(original residue number in PDB)
R314 A317
Binding residue
(residue number reindexed from 1)
R313 A316
Enzymatic activity
Catalytic site (original residue number in PDB)
H239 N240 G257
Catalytic site (residue number reindexed from 1)
H238 N239 G256
Enzyme Commision number
2.3.1.191
: UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase.
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:4ihg
,
PDBe:4ihg
,
PDBj:4ihg
PDBsum
4ihg
PubMed
24196711
UniProt
P21645
|LPXD_ECOLI UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (Gene Name=lpxD)
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