2iu9

X-ray diffraction
3.1Å resolution

Chlamydia trachomatis LpxD with 100mM UDPGlcNAc (Complex II)

Released:
Source organism: Chlamydia trachomatis
Primary publication:
Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis.
Proc Natl Acad Sci U S A 104 4321-6 (2007)
PMID: 17360522

Function and Biology Details

Reaction catalysed:
A (3R)-3-hydroxyacyl-[acyl-carrier-protein] + a UDP-3-O-((3R)-hydroxyacyl)-alpha-D-glucosamine = a UDP-2-N,3-O-bis((3R)-3-hydroxyacyl)-alpha-D-glucosamine + a holo-[acyl-carrier-protein]

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-533679 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-3-O-acylglucosamine N-acyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 374 amino acids
Theoretical weight: 40.63 KDa
Source organism: Chlamydia trachomatis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CD76 (Residues: 1-354; Coverage: 100%)
Gene names: CT_243, lpxD
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P41212
Unit cell:
a: 98.871Å b: 98.872Å c: 283.053Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.281
Expression system: Escherichia coli BL21(DE3)