8q2p

X-ray diffraction
1.9Å resolution

Structure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coli by using Se-MAG for the the lipid cubic phase crystallization

Released:

Function and Biology Details

Reaction catalysed:
A phosphoglycerolipid + an [apolipoprotein]-S-1,2-diacyl-sn-glyceryl-L-cysteine = a 1-lyso-phosphoglycerolipid + a [lipoprotein]-N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteine
Biochemical function:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-150121 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein N-acyltransferase Chain: A
Molecule details ›
Chain: A
Length: 510 amino acids
Theoretical weight: 56.82 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P23930 (Residues: 1-510; Coverage: 100%)
Gene names: JW0654, b0657, cutE, lnt
Sequence domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 156.61Å b: 48.79Å c: 75.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.224
Expression system: Escherichia coli