› 8hlm

X-ray diffraction
2.52Å resolution

Crystal structure of p53/BCL2 fusion complex (complex 2)

Released:
DOI: 10.2210/pdb8hlm/pdb
PDB entry 8hlm coloured by chain, front view.
PDB entry 8hlm coloured by chain, side view.
PDB entry 8hlm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of p53/BCL-2 complex suggest a mechanism for p53 to antagonize BCL-2 activity.
Wei H, Wang H, Wang G, Qu L, Jiang L, Dai S, Chen X, Zhang Y, Chen Z, Li Y, Guo M, Chen Y
OpenAccess logo Nat Commun 14 4300 (2023)
PMID: 37463921

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-222238 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cellular tumor antigen p53 Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 22.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04637 (Residues: 95-290; Coverage: 50%)
Gene names: P53, TP53
Sequence domains: P53 DNA-binding domain
Apoptosis regulator Bcl-2 Chain: B
Molecule details ›
Chain: B
Length: 177 amino acids
Theoretical weight: 19.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10415 (Residues: 10-35, 92-203; Coverage: 58%)
  • Best match: P10415-2 (Residues: 10-35, 92-195)
Gene name: BCL2
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL02U1
Spacegroup: P212121
Unit cell:
a: 45.61Å b: 70.336Å c: 127.158Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.234 0.29
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Amino Acid Derivatives of Ginsenoside AD-2 Induce HepG2 Cell Apoptosis by Affecting the Cytoskeleton.
Lin et al. (2023)
5 more