8HOH: Bcl-2 G101V

Crystal structure of Bcl-2 G101V in complex with sonrotoclax. Determined by X-ray diffraction at 1.9 Å resolution. Released 17 Jan 2024.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
1
Atoms
1,284
Mol. weight
19.91 kDa
Ligands
98I
Released
17 Jan 2024

Explore 8HOH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8HOH contains 9 α-helices and 0 β-strands across 1 chain. 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

ElementResiduesLengthSheet
α-helix11-2515
α-helix91-10717
α-helix109-1179
α-helix126-13712
α-helix144-16320
α-helix168-18013
α-helix181-1855
α-helix186-1916
α-helix195-2028

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apoptosis regulator Bcl-2Aprotein162Homo sapiensP10415 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8HOH_1 Apoptosis regulator Bcl-2 (chains A)
SRTGYDNREIVMKYIHYKLSQRGYEWDAGDDVEENRTEAPEGTESEVVHLTLRQAVDDFS
RRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNRE
MSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMR

Ligands and cofactors

IDNameFormulaCopies
98I~{N}-[4-[(4-methyl-4-oxidanyl-cyclohexyl)methylamino]-3-nitro-phenyl]sulfonyl-4…C49 H59 N7 O7 S1

Primary citation

Sonrotoclax overcomes BCL2 G101V mutation-induced venetoclax resistance in preclinical models of hematologic malignancy. Liu, J., Li, S., Wang, Q. et al. Blood (2024) 143:1825-1836. DOI 10.1182/blood.2023019706 · PubMed

Other PDB entries of the same protein (UniProt P10415 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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