› 5vx3

X-ray diffraction
1.94Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128973 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bcl-2-like protein 1 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 158 amino acids
Theoretical weight: 17.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07817 (Residues: 1-209; Coverage: 66%)
Gene names: BCL2L, BCL2L1, BCLX
Sequence domains:
Bcl-2-like protein 11 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 26 amino acids
Theoretical weight: 3.24 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: O43521 (Residues: 141-166; Coverage: 13%)
Gene names: BCL2L11, BIM
Sequence domains: Bcl-x interacting, BH3 domain

Ligands and Environments

1 bound ligand:
Ligand EDO 13 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: C2
Unit cell:
a: 125.661Å b: 68.811Å c: 102.83Å
α: 90° β: 125.35° γ: 90°
R-values:
R R work R free
0.196 0.194 0.243
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

11 review citations

Mitochondria as multifaceted regulators of cell death.
Bock et al. (2020)
10 more

1 mention without citation

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