4BD8: Apoptosis regulator bax

Name: PDB 4BD8: Bax domain swapped dimer induced by BimBH3 with CHAPS
Published: 2013-02-13
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: apoptosis

Bax domain swapped dimer induced by BimBH3 with CHAPS. Determined by X-ray diffraction at 2.22 Å resolution. Released 13 Feb 2013.

Method: X-ray diffraction
Resolution: 2.22 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 4,664
Mol. weight: 77.51 kDa
Ligands: PR
Released: 13 Feb 2013

Explore 4BD8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4BD8 contains 32 α-helices and 0 β-strands across 4 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

Element	Residues	Length
α-helix	16-36	21
α-helix	54-70	17
α-helix	74-81	8
α-helix	88-99	12
α-helix	107-143	37
α-helix	144-148	5
α-helix	149-154	6
α-helix	158-163	6

Chain B: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	16-34	19
α-helix	48-51	4
α-helix	54-70	17
α-helix	74-80	7
α-helix	89-98	10
α-helix	107-143	37
α-helix	144-148	5
α-helix	149-154	6
α-helix	158-163	6

Chain C: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	19-35	17
α-helix	54-71	18
α-helix	77-80	4
α-helix	89-99	11
α-helix	107-143	37
α-helix	144-148	5
α-helix	149-152	4
α-helix	157-160	4

Chain D: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	16-34	19
α-helix	56-71	16
α-helix	76-80	5
α-helix	92-99	8
α-helix	107-147	41
α-helix	149-153	5
α-helix	157-163	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apoptosis regulator bax	A, B, C, D	protein	174	HOMO SAPIENS	Q07812 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4BD8_1 APOPTOSIS REGULATOR BAX (chains A, B, C, D)
MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLS
ESLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKL
VLKALSTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQGSS

Ligands and cofactors

ID	Name	Formula	Copies
PR	Praseodymium ion	Pr	2

Water and common crystallization additives (EDO) are not listed.

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:

4ZIE 1.8 Å, Crystal Structure of core/latch dimer of Bax in complex with BimBH3
5W60 1.8 Å, Crystal structure of BAXP168G monomer cryo-protected with ethylene glycol
4S0O 1.9 Å, Crystal Structure of the Autoinhibited Dimer of Pro-apoptotic BAX (I)
5W5Z 2.0 Å, Crystal structure of BAXP168G in complex with an activating antibody at high resolution
6EB6 2.02 Å, Crystal structure of BAX W139A monomer
8SRX 2.09 Å, Crystal structure of BAK-BAX heterodimer with lysoPC
8G1T 2.09 Å, Crystal structure of Bax core domain BH3-groove dimer - tetrameric fraction P21
6TRR 2.12 Å, Structural insight into tanapoxvirus mediated inhibition of apoptosis
4ZII 2.19 Å, Crystal Structure of core/latch dimer of BaxI66A in complex with BidBH3
4ZIG 2.2 Å, Crystal Structure of core/latch dimer of Bax in complex with BidBH3mini
8SPF 2.2 Å, Crystal structure of Bax core domain BH3-groove dimer - hexameric fraction with…
4BD2 2.21 Å, Bax domain swapped dimer in complex with BidBH3

Browse structure collections

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