X-ray diffraction
2.9Å resolution

Crystal Structure of Human Phosphatidylcholine Transfer Protein in Complex with Dilinoleoylphosphatidylcholine (Seleno-Met Protein)


Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Phosphatidylcholine transfer protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 214 amino acids
Theoretical weight: 25.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q9UKL6 (Residues: 1-214; Coverage: 100%)
Gene names: PCTP, STARD2
Sequence domains: START domain
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9A
Spacegroup: P4212
Unit cell:
a: 134.7Å b: 134.7Å c: 82.7Å
α: 90° β: 90° γ: 90°
R R work R free
0.234 0.231 0.293
Expression system: Escherichia coli