› 3inq

X-ray diffraction
2Å resolution

Crystal structure of BCL-XL in complex with W1191542

Released:
DOI: 10.2210/pdb3inq/pdb
PDB entry 3inq coloured by chain, front view.
PDB entry 3inq coloured by chain, side view.
PDB entry 3inq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformational changes in Bcl-2 pro-survival proteins determine their capacity to bind ligands.
Lee EF, Czabotar PE, Yang H, Sleebs BE, Lessene G, Colman PM, Smith BJ, Fairlie WD
J Biol Chem 284 30508-17 (2009)
PMID: 19726685

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170525 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bcl-2-like protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 158 amino acids
Theoretical weight: 17.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07817 (Residues: 1-209; Coverage: 66%)
Gene names: BCL2L, BCL2L1, BCLX
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand X0J 2 x X0J
Ligand EDO 11 x EDO
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 62.588Å b: 68.214Å c: 71.401Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy.
Czabotar et al. (2014)
17 more

12 mentions without citation

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