9LGU: Bcl-xL
Crystal structure of Bcl-xL in complex with stapled HRK peptide. Determined by X-ray diffraction at 2.97 Å resolution. Released 6 Aug 2025.
- Method
- X-ray diffraction
- Resolution
- 2.97 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 8,005
- Mol. weight
- 164.1 kDa
- Ligands
- MG
- Released
- 6 Aug 2025
Explore 9LGU in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9LGU contains 63 α-helices and 0 β-strands across 12 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: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-18 | 16 | |
| α-helix | 24-26 | 3 | |
| α-helix | 84-104 | 21 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-130 | 12 | |
| α-helix | 137-156 | 20 | |
| α-helix | 162-173 | 12 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-184 | 6 | |
| α-helix | 188-194 | 7 | |
Chains B, D and M: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 29-48 | 20 | |
Chain C: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-18 | 16 | |
| α-helix | 24-26 | 3 | |
| α-helix | 84-104 | 21 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-130 | 12 | |
| α-helix | 137-156 | 20 | |
| α-helix | 162-173 | 12 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-183 | 5 | |
| α-helix | 188-194 | 7 | |
Chain E: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-19 | 17 | |
| α-helix | 84-104 | 21 | |
| α-helix | 119-130 | 12 | |
| α-helix | 137-156 | 20 | |
| α-helix | 160-162 | 3 | |
| α-helix | 163-173 | 11 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-183 | 5 | |
| α-helix | 188-194 | 7 | |
Chains F and H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-49 | 22 | |
Chain G: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-19 | 17 | |
| α-helix | 24-26 | 3 | |
| α-helix | 84-104 | 21 | |
| α-helix | 119-130 | 12 | |
| α-helix | 137-156 | 20 | |
| α-helix | 160-162 | 3 | |
| α-helix | 163-173 | 11 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-184 | 6 | |
| α-helix | 187-195 | 9 | |
Chain I: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-19 | 19 | |
| α-helix | 24-26 | 3 | |
| α-helix | 84-104 | 21 | |
| α-helix | 119-130 | 12 | |
| α-helix | 137-156 | 20 | |
| α-helix | 161-173 | 13 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-184 | 6 | |
| α-helix | 187-195 | 9 | |
Chain K: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-19 | 19 | |
| α-helix | 24-26 | 3 | |
| α-helix | 84-104 | 21 | |
| α-helix | 119-130 | 12 | |
| α-helix | 137-156 | 20 | |
| α-helix | 162-173 | 12 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-183 | 5 | |
| α-helix | 187-194 | 8 | |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Bcl-2-like protein 1 | A, C, E, G, I, K | protein | 218 | Homo sapiens | Q07817 (AlphaFold model) |
| Activator of apoptosis harakiri | B, D, F, H, L, M | protein | 24 | Homo sapiens | O00198 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G, I, K), FASTA
>9LGU_1 Bcl-2-like protein 1 (chains A, C, E, G, I, K)
SMSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHL
ADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTA
YQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLE
PWIQENGGWDTFVELYGNNAAAESRKGQERLEHHHHHH
Sequence of entity 2 (B, D, F, H, L, M), FASTA
>9LGU_2 Activator of apoptosis harakiri (chains B, D, F, H, L, M)
SSAAQLLALRLKLLGDELHQRTMW
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MG | Magnesium ion | Mg | 5 |
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:
- 7JGW 1.3 Å, Crystal structure of BCL-XL in complex with COMPOUND 1620116, CRYSTAL FORM 1
- 3SP7 1.4 Å, Crystal Structure of Bcl-xL bound to BM903
- 7YAA 1.4 Å, Crystal structure analysis of cp3 bound BCLxl
- 7LH7 1.41 Å, Crystal structure of BCL-XL in complex with a benzothiazole-based inhibitor
- 9IGG 1.5 Å, Structure of human Bcl-xL in complex with small molecule inhibitor
- 4QVF 1.53 Å, Crystal structure of Bcl-xL in complex with BIM BH3 domain
- 4A1U 1.54 Å, Crystal structure of alpha-beta-foldamer 2c in complex with Bcl-xL
- 6VWC 1.6 Å, Crystal structure of Bcl-xL in complex with tetrahydroisoquinoline-pyridine based…
- 6O0K 1.62 Å, crystal structure of BCL-2 with venetoclax
- 3SPF 1.7 Å, Crystal Structure of Bcl-xL bound to BM501
- 9I9E 1.7 Å, Structure of human Bcl-xL in complex with small molecule inhibitor
- 9O14 1.73 Å, Crystal Structure of BCL-2 in complex with a stapled BAD BH3 peptide BAD SAHB 4.2
Browse structure collections
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