› 6mvd

X-ray diffraction
3.1Å resolution

Crystal structure of Lecithin:cholesterol acyltransferase (LCAT) in complex with isopropyl dodec-11-enylfluorophosphonate (IDFP) and a small molecule activator

Released:
DOI: 10.2210/pdb6mvd/pdb
PDB entry 6mvd coloured by chain, front view.
PDB entry 6mvd coloured by chain, side view.
PDB entry 6mvd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for activation of lecithin:cholesterol acyltransferase by a compound that increases HDL cholesterol.
Manthei KA, Yang SM, Baljinnyam B, Chang L, Glukhova A, Yuan W, Freeman LA, Maloney DJ, Schwendeman A, Remaley AT, Jadhav A, Tesmer JJ
Elife 7 (2018)
PMID: 30479275

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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137486 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylcholine-sterol acyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 43.69 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P04180 (Residues: 45-421; Coverage: 91%)
Gene name: LCAT
Sequence domains: Lecithin:cholesterol acyltransferase
Structure domains: alpha/beta hydrolase

Ligands and Environments

5 bound ligands:
Ligand NAG 5 x NAG
Ligand H9A 2 x H9A
Ligand H94 2 x H94
Ligand SO4 6 x SO4
Ligand NI 1 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: C2
Unit cell:
a: 134.697Å b: 106.377Å c: 117.823Å
α: 90° β: 125.45° γ: 90°
R-values:
R R work R free
0.195 0.193 0.239
Expression system: Homo sapiens

Quick links

Citations

1 review citation

Regulation of cholesterol homeostasis in health and diseases: from mechanisms to targeted therapeutics.
Duan et al. (2022)
9 other articles

7 mentions without citation

Structural analysis of lecithin:cholesterol acyltransferase bound to high density lipoprotein particles.
Manthei et al. (2020)
6 more