4S0O: Autoinhibited Dimer of Pro-apoptotic BAX

Crystal Structure of the Autoinhibited Dimer of Pro-apoptotic BAX (I). Determined by X-ray diffraction at 1.9 Å resolution. Released 20 Jul 2016.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
2
Atoms
2,878
Mol. weight
42.33 kDa
Released
20 Jul 2016

Explore 4S0O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4S0O contains 25 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: 12 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix16-3419
α-helix43-453
α-helix46-516
α-helix54-7118
α-helix74-818
α-helix89-9911
α-helix107-12620
α-helix131-14313
α-helix144-1485
α-helix149-1546
α-helix158-1647
α-helix170-19122
Chain B: 13 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix16-3419
α-helix43-453
α-helix46-516
α-helix54-7118
α-helix74-818
α-helix89-9911
α-helix107-12620
α-helix131-14313
α-helix144-1485
α-helix149-1546
α-helix158-1603
α-helix161-1644
α-helix170-19122

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apoptosis regulator BAXA, Bprotein192Homo sapiensQ07812 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4S0O_1 Apoptosis regulator BAX (chains A, B)
MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLS
ECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKL
VLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTGTWQTVTIFVAGV
LTASLTIWKKMG

Primary citation

An Autoinhibited Dimeric Form of BAX Regulates the BAX Activation Pathway. Garner, T.P., Reyna, D.E., Priyadarshi, A. et al. Mol Cell (2016) 63:485-497. DOI 10.1016/j.molcel.2016.06.010 · 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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