X-ray diffraction
2.2Å resolution

2.2 Angstrom Crystal Structure of C Terminal Truncated Human Apolipoprotein A-I Reveals the Assembly of HDL by Dimerization.


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Truncated apolipoprotein A-I Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 21.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P02647 (Residues: 25-208; Coverage: 74%)
Gene name: APOA1
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P21212
Unit cell:
a: 108.333Å b: 30.178Å c: 69.576Å
α: 90° β: 90° γ: 90°
R R work R free
0.236 0.23 0.28
Expression system: Escherichia coli BL21(DE3)