6o0m

X-ray diffraction
1.75Å resolution

crystal structure of BCL-2 F104L mutation with venetoclax

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (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:

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