› 6f46

Solution NMR

Structure of the transmembrane helix of BclxL in phospholipid nanodiscs

Released:
DOI: 10.2210/pdb6f46/pdb
PDB entry 6f46 coloured by chain, ensemble of 20 models, front view.
PDB entry 6f46 coloured by chain, ensemble of 20 models, side view.
PDB entry 6f46 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Production and Structural Analysis of Membrane-Anchored Proteins in Phospholipid Nanodiscs.
Raltchev K, Pipercevic J, Hagn F
Chemistry 24 5493-5499 (2018)
PMID: 29457664

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bcl-2-like protein 1 Chain: A
Molecule details ›
Chain: A
Length: 35 amino acids
Theoretical weight: 3.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07817 (Residues: 202-233; Coverage: 14%)
Gene names: BCL2L, BCL2L1, BCLX

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 34%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Natural Occurring and Engineered Enzymes for Peptide Ligation and Cyclization.
Nuijens et al. (2019)
2 more

5 mentions without citation

The Structural Biology of Bcl-xL.
Lee et al. (2019)
4 more