PDBe 1gw4

Solution NMR

THE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-I DETERMINED BY NMR SPECTROSCOPY, 1 STRUCTURE

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Truncated apolipoprotein A-I Chain: A
Molecule details ›
Chain: A
Length: 46 amino acids
Theoretical weight: 5.15 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02647 (Residues: 166-211; Coverage: 19%)
Gene name: APOA1
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY CALCULATIONS USING NOE-DERIVED DISTANCES
Expression system: Not provided