2JCN: BAK1 - a mitochondrial apoptosis regulator

The crystal structure of BAK1 - a mitochondrial apoptosis regulator. Determined by X-ray diffraction at 1.8 Å resolution. Released 4 Jan 2007.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
HOMO SAPIENS
Chains
1
Atoms
1,375
Mol. weight
19.42 kDa
Released
4 Jan 2007

Explore 2JCN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2JCN contains 8 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: 8 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix24-4724
α-helix58-603
α-helix70-10031
α-helix107-11812
α-helix125-14420
α-helix151-16414
α-helix167-1737
α-helix177-1826

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bcl-2 homologous antagonist/killerAprotein172HOMO SAPIENSQ16611 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2JCN_1 BCL-2 HOMOLOGOUS ANTAGONIST/KILLER (chains A)
SMSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQL
AIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYRL
ALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNGPILN

Primary citation

The Crystal Structure of Bak1 - an Apoptosis Trigger in the Mitochondrial Outer Membrane. Moche, M., Stenmark, P., Arrowsmith, C. et al. To be published.

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

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