Structure of PDB 2iu9 Chain C

Receptor sequence
>2iu9C (length=346) Species: 813 (Chlamydia trachomatis) [Search protein sequence]
QSTYSLEQLADFLKVEFQGNGATLLSGVEEIEEAKTAHITFLDNEKYAKH
LKSSEAGAIIISRTQFQKYRDLNKNFLITSESPSLVFQKCLELFITPVDS
GFPGIHPTAVIHPTAIIEDHVCIEPYAVVCQHAHVGSACHIGSGSVIGAY
STVGEHSYIHPRVVIRERVSIGKRVIIQPGAVIGSCGFGYVTSAFGQHKH
LKHLGKVIIEDDVEIGANTTIDRGRFKHSVVREGSKIDNLVQIAHQVEVG
QHSMIVAQAGIAGSTKIGNHVIIGGQAGITGHICIADHVIMMAQTGVTKS
ITSPGIYGGAPARPYQEIHRQVAKVRNLPRLEERIAALEKLVQKLE
3D structure
PDB2iu9 Structure and Reactivity of Lpxd, the N-Acyltransferase of Lipid a Biosynthesis
ChainC
Resolution3.1 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 C D240 A295 Q296 D238 A293 Q294
BS02 UD1 C E32 I33 E34 F43 L44 D45 Y49 E30 I31 E32 F41 L42 D43 Y47
BS03 PLM C Q244 A246 G262 I263 A264 T282 Q242 A244 G260 I261 A262 T280
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

View graph for
Molecular Function
View graph for
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)

[Back to BioLiP]