9LI8: Bcl-xL

Crystal structure of Bcl-xL in complex with HRK BH3 peptide. Determined by X-ray diffraction at 2.32 Å resolution. Released 6 Aug 2025.

Method
X-ray diffraction
Resolution
2.32 Å
Organism
Homo sapiens
Chains
2
Atoms
1,426
Mol. weight
27.28 kDa
Released
6 Aug 2025

Explore 9LI8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9LI8 contains 12 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 11 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix4-1916
α-helix24-263
α-helix83-10422
α-helix119-13012
α-helix137-15620
α-helix161-17313
α-helix174-1785
α-helix179-1846
α-helix187-1959
α-helix196-1983
α-helix199-2035
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix28-4922

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bcl-2-like protein 1Aprotein217Homo sapiensQ07817 (AlphaFold model)
Activator of apoptosis harakiriBprotein25Homo sapiensO00198 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9LI8_1 Bcl-2-like protein 1 (chains A)
MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLA
DSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAY
QSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEP
WIQENGGWDTFVELYGNNAAAESRKGQERLEHHHHHH
Sequence of entity 2 (B), FASTA
>9LI8_2 Activator of apoptosis harakiri (chains B)
SSAAQLTAARLKALGDELHQRTMWR

Primary citation

Molecular mechanisms underlying HRK interaction with BCL-XL and BCL-2 reveal specificity determinants for BH3 mimetics. Wang, J., Guo, M., Dai, S. et al. iScience (2025) 28:113309-113309. DOI 10.1016/j.isci.2025.113309 · PubMed

Other PDB entries of the same protein (UniProt Q07817 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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