› 1bxl

Solution NMR

STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE

Released:
DOI: 10.2210/pdb1bxl/pdb
PDB entry 1bxl coloured by chain, front view.
PDB entry 1bxl coloured by chain, side view.
PDB entry 1bxl coloured by chain, top view.
Source organisms:
Primary publication:
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis.
Sattler M, Liang H, Nettesheim D, Meadows RP, Harlan JE, Eberstadt M, Yoon HS, Shuker SB, Chang BS, Minn AJ, Thompson CB, Fesik SW
Science 275 983-6 (1997)
PMID: 9020082

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170521 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bcl-2-like protein 1 Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 24.88 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07817 (Residues: 1-210; Coverage: 90%)
Gene names: BCL2L, BCL2L1, BCLX
Sequence domains:
Structure domains: Blc2-like
Bcl-2 homologous antagonist/killer Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.73 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q16611 (Residues: 72-87; Coverage: 8%)
Gene names: BAK, BAK1, BCL2L7, CDN1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

245 review citations

The biochemistry of apoptosis.
Hengartner MO. (2000)
244 more

82 mentions without citation

Understanding protein non-folding.
Uversky et al. (2010)
81 more