4dot

X-ray diffraction
1.96Å resolution

Crystal structure of human HRASLS3.

Released:

Function and Biology Details

Reactions catalysed:
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

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-156883 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A and acyltransferase 3 Chain: A
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 15.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53816 (Residues: 1-132; Coverage: 82%)
Gene names: HRASLS3, HREV107, PLA2G16, PLAAT3
Sequence domains: Lecithin retinol acyltransferase
Structure domains: endopeptidase domain like (from Nostoc punctiforme)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P3121
Unit cell:
a: 62.446Å b: 62.446Å c: 73.922Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.203 0.216
Expression system: Escherichia coli