› 1by6

Solution NMR

Peptide of human apolipoprotein C-II

Released:
DOI: 10.2210/pdb1by6/pdb
PDB entry 1by6 coloured by chain, ensemble of 19 models, front view.
PDB entry 1by6 coloured by chain, ensemble of 19 models, side view.
PDB entry 1by6 coloured by chain, ensemble of 19 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine.
Storjohann R, Rozek A, Sparrow JT, Cushley RJ
Biochim Biophys Acta 1486 253-64 (2000)
PMID: 10903476

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135996 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein C-II Chain: A
Molecule details ›
Chain: A
Length: 36 amino acids
Theoretical weight: 3.97 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02655 (Residues: 66-101; Coverage: 46%)
Gene names: APC2, APOC2
Sequence domains: Apolipoprotein C-II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY/SIMULATED ANNEALING/RELAXATION MATRIX REFINEMENT
Expression system: Not provided

Quick links

Citations

5 review citations

A review of the role of apolipoprotein C-II in lipoprotein metabolism and cardiovascular disease.
Kei et al. (2012)
4 more

1 mention without citation

How does averaging affect protein structure comparison on the ensemble level?
Zagrovic et al. (2004)