› 1oeg

Solution NMR

PEPTIDE OF HUMAN APOE RESIDUES 267-289, NMR, 5 STRUCTURES AT PH 6.0, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:90

Released:
DOI: 10.2210/pdb1oeg/pdb
PDB entry 1oeg coloured by chain, ensemble of 5 models, front view.
PDB entry 1oeg coloured by chain, ensemble of 5 models, side view.
PDB entry 1oeg coloured by chain, ensemble of 5 models, top view.
Source organism: Homo sapiens
Primary publication:
Conformations of human apolipoprotein E(263-286) and E(267-289) in aqueous solutions of sodium dodecyl sulfate by CD and 1H NMR.
Wang G, Pierens GK, Treleaven WD, Sparrow JT, Cushley RJ
Biochemistry 35 10358-66 (1996)
PMID: 8756691

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-135991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein E Chain: A
Molecule details ›
Chain: A
Length: 23 amino acids
Theoretical weight: 2.53 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02649 (Residues: 285-307; Coverage: 8%)
Gene name: APOE

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

5 review citations

Structural models of human apolipoprotein A-I: a critical analysis and review.
Brouillette et al. (2001)
4 more

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)