Structure of PDB 2iu9 Chain B

Receptor sequence
>2iu9B (length=345) Species: 813 (Chlamydia trachomatis) [Search protein sequence]
MSQSTYSLEQLADFLKVEFQGNGATLLSGVEEIEEAKTAHITFLDNEKYA
KHLKSSEAGAIIISRTQFQKYRDLNKNFLITSESPSLVFQKCLELFITPV
DSGFPGIHPTAVIHPTAIIEDHVCIEPYAVVCQHAHVGSACHIGSGSVIG
AYSTVGEHSYIHPRVVIRERVSIGKRVIIQPGAVIGSCGFGYVTSAFGQH
KHLKHLGKVIIEDDVEIGANTTIDRGRFKHSVVREGSKIDNLVQIAHQVE
VGQHSMIVAQAGIAGSTKIGNHVIIGGQAGITGHICIADHVIMMAQTGVT
KSITSPGIYGGAPARPYQEIHRQVAKVRNLPRLEERIAALEKLVQ
3D structure
PDB2iu9 Structure and Reactivity of Lpxd, the N-Acyltransferase of Lipid a Biosynthesis
ChainB
Resolution3.1 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 PLM B D240 M294 A295 D240 M294 A295
BS02 UD1 B E32 I33 F43 L44 N46 Y49 E32 I33 F43 L44 N46 Y49
BS03 PLM B Q244 A246 G262 I263 A264 G280 I281 G298 A312 Q244 A246 G262 I263 A264 G280 I281 G298 A312
BS04 UD1 B F228 H247 Q248 G283 H284 F228 H247 Q248 G283 H284
Gene Ontology
Molecular Function
GO:0016410 N-acyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0009245 lipid A biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2iu9, PDBe:2iu9, PDBj:2iu9
PDBsum2iu9
PubMed17360522
UniProtP0CD76|LPXD_CHLTR UDP-3-O-acylglucosamine N-acyltransferase (Gene Name=lpxD)

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