Structure of PDB 4ihg Chain E

Receptor sequence

>4ihgE (length=337) Species: 83333 (Escherichia coli K-12)

ASIRLADLAQQLDAELHGDGDIVITGVASMQSAQTGHITFMVNPKYREHL
GLCQASAVVMTQDDLPFAKSAALVVKNPYLTYARMAQILDTTPQPAQNIA
PSAVIDATAKLGNNVSIGANAVIESGVELGDNVIIGAGCFVGKNSKIGAG
SRLWANVTIYHEIQIGQNCLIQSGTVVGADGFGYANDRGNWVKIPQIGRV
IIGDRVEIGACTTIDRGALDDTIIGNGVIIDNQCQIAHNVVIGDNTAVAG
GVIMAGSLKIGRYCMIGGASVINGHMEICDKVTVTGMGMVMRPITEPGVY
SSGIPLQPNKVWRKTAALVMNIDDMSKRLKSLERKVN

3D structure

• PDB: 4ihg Chasing acyl carrier protein through a catalytic cycle of lipid A production.
• Chain: E
• Resolution: 2.89 Å

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.

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	peptide	E	R314 A317	R313 A316

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

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)