9CPE: Bcl-2 homologous antagonist/killer

Structural basis of BAK sequestration by MCL-1 and consequences for apoptosis initiation. Determined by X-ray diffraction at 1.49 Å resolution. Released 4 Jun 2025.

Method
X-ray diffraction
Resolution
1.49 Å
Organism
Homo sapiens
Chains
1
Atoms
1,411
Mol. weight
18.82 kDa
Released
4 Jun 2025

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

Secondary structure: helices and β-sheets

9CPE contains 10 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: 10 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix21-4323
α-helix58-614
α-helix63-642
α-helix70-8516
α-helix87-9913
α-helix107-11812
α-helix125-14622
α-helix151-16414
α-helix167-1737
α-helix177-1826

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bcl-2 homologous antagonist/killerAprotein167Homo sapiensQ16611 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9CPE_1 Bcl-2 homologous antagonist/killer (chains A)
PSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPAQPSSTMGQVGRQLA
IIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWRRVVALLGFGYRLA
LHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNG

Primary citation

Structural basis of BAK sequestration by MCL-1 in apoptosis. Srivastava, S., Sekar, G., Ojoawo, A. et al. Mol Cell (2025) 85:1606-1623.e10. DOI 10.1016/j.molcel.2025.03.013 · PubMed

Other PDB entries of the same protein (UniProt Q16611 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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