Structure of PDB 4ihh Chain B

Receptor sequence

>4ihhB (length=335) Species: 83333 (Escherichia coli K-12)

SIRLADLAQQLDAELHGDGDIVITGVASMQSAQTGHITFMVNPKYREHLG
LCQASAVVMTQDDLPFAKSAALVVKNPYLTYARMAQILDTTPQPAQNIAP
SAVIDATAKLGNNVSIGANAVIESGVELGDNVIIGAGCFVGKNSKIGAGS
RLWANVTIYHEIQIGQNCLIQSGTVVGADGFGYANDRGNWVKIPQIGRVI
IGDRVEIGACTTIDRGALDDTIIGNGVIIDNQCQIAHNVVIGDNTAVAGG
VIMAGSLKIGRYCMIGGASVINGHMEICDKVTVTGMGMVMRPITEPGVYS
SGIPLQPNKVWRKTAALVMNIDDMSKRLKSLERKV

3D structure

• PDB: 4ihh Chasing acyl carrier protein through a catalytic cycle of lipid A production.
• Chain: B
• Resolution: 2.132 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H239 N240 G257
• Catalytic site (residue number reindexed from 1): H237 N238 G255
• 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	PNS	B	N310 R314	N308 R312
BS02	PNS	B	N274 V291 M292	N272 V289 M290
BS03	PNS	B	T286 G287	T284 G285

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:4ihh, PDBe:4ihh, PDBj:4ihh
• PDBsum: 4ihh
• PubMed: 24196711
• UniProt: P21645|LPXD_ECOLI UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (Gene Name=lpxD)