9O15: BCL-2 (G101V) mutant
Crystal Structure of BCL-2 (G101V) mutant in complex with a stapled BAD BH3 peptide BAD SAHB 4.2. Determined by X-ray diffraction at 1.99 Å resolution. Released 8 Oct 2025.
- Method
- X-ray diffraction
- Resolution
- 1.99 Å
- Organism
- Homo sapiens
- Chains
- 14
- Atoms
- 8,844
- Mol. weight
- 138.65 kDa
- Released
- 8 Oct 2025
Explore 9O15 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9O15 contains 62 α-helices and 0 β-strands across 14 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: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-25 | 15 | |
| α-helix | 91-107 | 17 | |
| α-helix | 109-118 | 10 | |
| α-helix | 123-137 | 15 | |
| α-helix | 144-163 | 20 | |
| α-helix | 168-180 | 13 | |
| α-helix | 181-185 | 5 | |
| α-helix | 186-191 | 6 | |
| α-helix | 194-202 | 9 | |
Chain B: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 304-321 | 18 | |
Chain C: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-25 | 15 | |
| α-helix | 91-107 | 17 | |
| α-helix | 109-119 | 11 | |
| α-helix | 123-137 | 15 | |
| α-helix | 144-163 | 20 | |
| α-helix | 168-180 | 13 | |
| α-helix | 181-185 | 5 | |
| α-helix | 186-191 | 6 | |
| α-helix | 194-202 | 9 | |
Chains D, J and L: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 304-322 | 19 | |
Chain E: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-25 | 15 | |
| α-helix | 91-107 | 17 | |
| α-helix | 109-118 | 10 | |
| α-helix | 126-137 | 12 | |
| α-helix | 144-163 | 20 | |
| α-helix | 167-180 | 14 | |
| α-helix | 181-185 | 5 | |
| α-helix | 186-191 | 6 | |
| α-helix | 194-202 | 9 | |
Chains F and H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 304-323 | 20 | |
Chain G: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-25 | 15 | |
| α-helix | 92-107 | 16 | |
| α-helix | 109-118 | 10 | |
| α-helix | 126-137 | 12 | |
| α-helix | 144-163 | 20 | |
| α-helix | 168-180 | 13 | |
| α-helix | 181-185 | 5 | |
| α-helix | 186-191 | 6 | |
| α-helix | 194-202 | 9 | |
Chain I: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-25 | 15 | |
| α-helix | 91-107 | 17 | |
| α-helix | 109-119 | 11 | |
| α-helix | 126-137 | 12 | |
| α-helix | 144-163 | 20 | |
| α-helix | 169-180 | 12 | |
| α-helix | 181-185 | 5 | |
| α-helix | 186-191 | 6 | |
| α-helix | 194-202 | 9 | |
2 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 |
|---|
| Apoptosis regulator Bcl-2,Bcl-2-like protein 1 | A, C, E, G, I, K | protein | 166 | Homo sapiens | P10415 (AlphaFold model), Q07817 (AlphaFold model) |
| stapled BAD BH3 peptide BAD SAHB 4.2 | B, D, F, H, J, L, M, N | protein | 23 | Homo sapiens | Q92934 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G, I, K), FASTA
>9O15_1 Apoptosis regulator Bcl-2,Bcl-2-like protein 1 (chains A, C, E, G, I, K)
MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDDVEENRTEAPEGTESEVVHLTLRQAV
DDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVES
VNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMR
Sequence of entity 2 (B, D, F, H, J, L, M, N), FASTA
>9O15_2 stapled BAD BH3 peptide BAD SAHB 4.2 (chains B, D, F, H, J, L, M, N)
XWLAQRLGRELRRLSDEFVDSFK
Primary citation
Structural insights into chemoresistance mutants of BCL-2 and their targeting by stapled BAD BH3 helices. DeAngelo, T.M., Adhikary, U., Korshavn, K.J. et al. Nat Commun (2025) 16:8623-8623. DOI 10.1038/s41467-025-63657-y · PubMed
Other PDB entries of the same protein (UniProt P10415 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8HTS 1.25 Å, Crystal structure of Bcl2 in complex with S-10r
- 6GL8 1.4 Å, Crystal structure of Bcl-2 in complex with the novel orally active inhibitor S55746
- 6QGG 1.5 Å, Structure of human Bcl-2 in complex with analogue of ABT-737
- 9IGG 1.5 Å, Structure of human Bcl-xL in complex with small molecule inhibitor
- 8HTR 1.6 Å, Crystal structure of Bcl2 in complex with S-9c
- 6O0K 1.62 Å, crystal structure of BCL-2 with venetoclax
- 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
- 9O16 1.73 Å, Crystal Structure of human BCL-2 (R129L) mutant in complex with a stapled BAD BH3…
- 6O0M 1.75 Å, crystal structure of BCL-2 F104L mutation with venetoclax
- 5VAU 1.75 Å, Bcl-2 complex with Beclin 1 BH3 domain
- 8VWX 1.77 Å, Human Bcl-2 (G101V Mutant)/Bcl-xL Chimera Fused to Maltose-Binding Protein
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