› 6o0m

X-ray diffraction
1.75Å resolution

crystal structure of BCL-2 F104L mutation with venetoclax

Released:
DOI: 10.2210/pdb6o0m/pdb
PDB entry 6o0m coloured by chain, front view.
PDB entry 6o0m coloured by chain, side view.
PDB entry 6o0m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations.
Birkinshaw RW, Gong JN, Luo CS, Lio D, White CA, Anderson MA, Blombery P, Lessene G, Majewski IJ, Thijssen R, Roberts AW, Huang DCS, Colman PM, Czabotar PE
OpenAccess logo Nat Commun 10 2385 (2019)
PMID: 31160589

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-145301 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apoptosis regulator Bcl-2; Bcl-2-like protein 1 Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 19.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P10415 (Residues: 1-34, 66-207; Coverage: 63%)
  • Canonical: Q07817 (Residues: 29-44; Coverage: 7%)
Gene names: BCL2, BCL2L, BCL2L1, BCLX
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand LBM 1 x LBM
Ligand PEG 4 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 33.69Å b: 48.27Å c: 87.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.172 0.218
Expression system: Escherichia coli BL21

Quick links

Citations

36 review citations

Targeting apoptosis in cancer therapy.
Carneiro et al. (2020)
35 more

2 mentions without citation

Structures of BCL-2 in complex with venetoclax reveal the molecular basis of resistance mutations.
Birkinshaw et al. (2019)
1 more