4q95

X-ray diffraction
2.2Å resolution

Crystal structure of HRASLS3/LRAT chimeric protein

Released:

Function and Biology Details

Reactions catalysed:
Phosphatidylcholine + retinol--[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester--[cellular-retinol-binding-protein]
Phosphatidylcholine + H(2)O = 2-acylglycerophosphocholine + a carboxylate
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lecithin retinol acyltransferase; Phospholipase A and acyltransferase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 149 amino acids
Theoretical weight: 16.96 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P53816 (Residues: 2-38, 59-129; Coverage: 67%)
  • Canonical: Q9JI60 (Residues: 76-106; Coverage: 13%)
Gene names: HRASLS3, HREV107, Lrat, PLA2G16, PLAAT3
Sequence domains: Lecithin retinol acyltransferase
Structure domains: endopeptidase domain like (from Nostoc punctiforme)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P43212
Unit cell:
a: 63.123Å b: 63.123Å c: 157.965Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.248
Expression system: Escherichia coli