We've built a new version of this page with an interactive 3D viewer. Try it out in beta and help us improve:

8rqr

X-ray diffraction
2.19Å resolution

In meso structure of apolipoprotein N-acyltransferase, Lnt, from Escherichia coli in 7.10 monoacylglycerol

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] +a glycerophospholipid = N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] + a 2-acyl-sn-glycero-3-phospholipid + H(+).
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: 532 amino acids
Theoretical weight: 59.28 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P23930 (Residues: 1-512; Coverage: 100%)
Gene names: JW0654, b0657, cutE, lnt
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I24
Unit cell:
a: 48.679Å b: 76.461Å c: 157.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.246
Expression system: Escherichia coli