9O16: Human BCL-2 (R129L) mutant

Crystal Structure of human BCL-2 (R129L) mutant in complex with a stapled BAD BH3 peptide BAD SAHB 4.2. Determined by X-ray diffraction at 1.73 Å resolution. Released 8 Oct 2025.

Method: X-ray diffraction
Resolution: 1.73 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,487
Mol. weight: 22.51 kDa
Ligands: NI
Released: 8 Oct 2025

Explore 9O16 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9O16 contains 11 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	11-24	14
α-helix	93-107	15
α-helix	109-119	11
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
α-helix	203-205	3

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	304-321	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apoptosis regulator Bcl-2,Bcl-2-like protein 1	A	protein	166	Homo sapiens	P10415 (AlphaFold model), Q07817 (AlphaFold model)
stapled BAD BH3 peptide BAD SAHB 4.2	B	protein	23	Homo sapiens	Q92934 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9O16_1 Apoptosis regulator Bcl-2,Bcl-2-like protein 1 (chains A)
MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDDVEENRTEAPEGTESEVVHLTLRQAG
DDFSRRYRRDFAEMSSQLHLTPFTARGLFATVVEELFRDGVNWGRIVAFFEFGGVMCVES
VNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMR

Sequence of entity 2 (B), FASTA

>9O16_2 stapled BAD BH3 peptide BAD SAHB 4.2 (chains B)
XWLAQRLGRELRRLSDEFVDSFK

Ligands and cofactors

ID	Name	Formula	Copies
NI	Nickel (II) ion	Ni	3

Water and common crystallization additives (SO4, IMD) are not listed.

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
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
6O0P 1.8 Å, crystal structure of BCL-2 G101A mutation with venetoclax

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