› 2lfm

Solution NMR

A partially folded structure of amyloid-beta(1 40) in an aqueous environment

Released:
DOI: 10.2210/pdb2lfm/pdb
PDB entry 2lfm coloured by chain, ensemble of 20 models, front view.
PDB entry 2lfm coloured by chain, ensemble of 20 models, side view.
PDB entry 2lfm coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
A partially folded structure of amyloid-beta(1-40) in an aqueous environment.
Vivekanandan S, Brender JR, Lee SY, Ramamoorthy A
Biochem Biophys Res Commun 411 312-6 (2011)
PMID: 21726530

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 40 Chain: A
Molecule details ›
Chain: A
Length: 40 amino acids
Theoretical weight: 4.34 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 672-711; Coverage: 5%)
Gene names: A4, AD1, APP
Sequence domains: Beta-amyloid peptide (beta-APP)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 49%
Refinement method: DGSA-distance geometry simulated annealing
Expression system: Not provided

Quick links

Citations

31 review citations

Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.
Nasica-Labouze et al. (2015)
30 more

48 mentions without citation

Amyloid beta: structure, biology and structure-based therapeutic development.
Chen et al. (2017)
47 more