4BD2: Bax domain swapped dimer

Bax domain swapped dimer in complex with BidBH3. Determined by X-ray diffraction at 2.21 Å resolution. Released 13 Feb 2013.

Method
X-ray diffraction
Resolution
2.21 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
1,455
Mol. weight
22.88 kDa
Released
13 Feb 2013

Explore 4BD2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4BD2 contains 10 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: 8 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix16-3621
α-helix54-7219
α-helix74-829
α-helix88-9912
α-helix107-14337
α-helix144-1485
α-helix149-1546
α-helix159-1646
Chain C: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix77-9620
α-helix97-993

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apoptosis regulator baxAprotein174HOMO SAPIENSQ07812 (AlphaFold model)
BH3-interacting domain death agonistCprotein34HOMO SAPIENSP55957 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4BD2_1 APOPTOSIS REGULATOR BAX (chains A)
MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLS
ESLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKL
VLKALSTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQGSS
Sequence of entity 2 (C), FASTA
>4BD2_2 BH3-INTERACTING DOMAIN DEATH AGONIST (chains C)
SESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGL

Primary citation

Bax Crystal Structures Reveal How Bh3 Domains Activate Bax and Nucleate its Oligomerization to Induce Apoptosis. Czabotar, P.E., Westphal, D., Dewson, G. et al. Cell (2013) 152:519. DOI 10.1016/J.CELL.2012.12.031 · PubMed

Other PDB entries of the same protein (UniProt Q07812 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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