4x96

X-ray diffraction
8.69Å resolution

Low resolution crystal structure of Lecithin:Cholesterol Acyltransferase (LCAT; residues 21-397)

Released:

Function and Biology Details

Reactions catalysed:
Phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H(2)O = 1-alkyl-sn-glycero-3-phosphocholine + acetate

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-137486 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Phosphatidylcholine-sterol acyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 383 amino acids
Theoretical weight: 43.69 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P04180 (Residues: 45-424; Coverage: 91%)
Gene name: LCAT
Sequence domains: Lecithin:cholesterol acyltransferase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: R3
Unit cell:
a: 367.258Å b: 367.258Å c: 187.069Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.21 0.229
Expression system: Homo sapiens