› 2lpc

Solution NMR

NMR STRUCTURE of Bcl-XL

Released:
DOI: 10.2210/pdb2lpc/pdb
PDB entry 2lpc coloured by chain, ensemble of 21 models, front view.
PDB entry 2lpc coloured by chain, ensemble of 21 models, side view.
PDB entry 2lpc coloured by chain, ensemble of 21 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR solution structure of a photoswitchable apoptosis activating Bak peptide bound to Bcl-xL.
Wysoczanski P, Mart RJ, Loveridge EJ, Williams C, Whittaker SB, Crump MP, Allemann RK
J Am Chem Soc 134 7644-7 (2012)
PMID: 22515821

Function and Biology Details

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

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: 185 amino acids
Theoretical weight: 21.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07817 (Residues: 1-209; Coverage: 73%)
Gene names: BCL2L, BCL2L1, BCLX
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

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Citations

8 review citations

Inhibition of α-helix-mediated protein-protein interactions using designed molecules.
Azzarito et al. (2013)
7 more

5 mentions without citation

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