Structure of PDB 2qiv Chain X

Receptor sequence
>2qivX (length=262) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MIDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVV
NGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIGDRNRIRESVTIHR
GTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDF
AIIGGMTAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIE
GLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVKAFT
DFFARSTRGLIR
3D structure
PDB2qiv Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase
ChainX
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H125 D126 G143
Catalytic site (residue number reindexed from 1) H125 D126 G143
Enzyme Commision number 2.3.1.129: acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-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 U21 X Q73 D74 L75 K76 H122 A124 H125 T140 G143 H144 Q161 Q73 D74 L75 K76 H122 A124 H125 T140 G143 H144 Q161
Gene Ontology
Molecular Function
GO:0008780 acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-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
Biological Process
GO:0008610 lipid biosynthetic process
GO:0009245 lipid A biosynthetic process
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:2qiv, PDBe:2qiv, PDBj:2qiv
PDBsum2qiv
PubMed17698807
UniProtP0A722|LPXA_ECOLI Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (Gene Name=lpxA)

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