› 1i5j

Solution NMR

NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS

Released:
DOI: 10.2210/pdb1i5j/pdb
PDB entry 1i5j coloured by chain, ensemble of 25 models, front view.
PDB entry 1i5j coloured by chain, ensemble of 25 models, side view.
PDB entry 1i5j coloured by chain, ensemble of 25 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
MacRaild CA, Hatters DM, Howlett GJ, Gooley PR
Biochemistry 40 5414-21 (2001)
PMID: 11331005

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: 79 amino acids
Theoretical weight: 8.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02655 (Residues: 23-101; Coverage: 100%)
Gene names: APC2, APOC2
Sequence domains: Apolipoprotein C-II
Structure domains: Apolipoprotein C-II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle and Cartesian dynamics
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins.
Saito et al. (2004)
13 more

2 mentions without citation

Structure-based machine-guided mapping of amyloid sequence space reveals uncharted sequence clusters with higher solubilities.
Louros et al. (2020)
1 more