8G1T: Apoptosis regulator BAX

Name: PDB 8G1T: Crystal structure of Bax core domain BH3-groove dimer - tetrameric fraction P21
Published: 2023-12-27
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: apoptosis

Crystal structure of Bax core domain BH3-groove dimer - tetrameric fraction P21. Determined by X-ray diffraction at 2.09 Å resolution. Released 27 Dec 2023.

Method: X-ray diffraction
Resolution: 2.09 Å
Organism: Homo sapiens
Chains: 8
Atoms: 4,513
Mol. weight: 71.84 kDa
Released: 27 Dec 2023

Explore 8G1T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8G1T contains 32 α-helices and 0 β-strands across 8 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.

Chains A and B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	56-72	17
α-helix	74-81	8
α-helix	88-99	12
α-helix	107-121	15

Chain C: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	55-72	18
α-helix	74-82	9
α-helix	88-99	12
α-helix	107-122	16

Chain D: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	55-72	18
α-helix	74-81	8
α-helix	88-99	12
α-helix	107-123	17

Chain E: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	57-72	16
α-helix	74-81	8
α-helix	88-99	12
α-helix	107-121	15

Chain F: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	57-72	16
α-helix	74-81	8
α-helix	88-99	12
α-helix	107-125	19

Chain G: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	56-72	17
α-helix	74-81	8
α-helix	88-99	12
α-helix	107-122	16

Chain H: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	56-72	17
α-helix	74-81	8
α-helix	88-99	12
α-helix	107-125	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apoptosis regulator BAX	A, B, C, D, E, F, G, H	protein	81	Homo sapiens	Q07812 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>8G1T_1 Apoptosis regulator BAX (chains A, B, C, D, E, F, G, H)
GPLGSDASTKKLSESLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNW
GRVVALFYFASKLVLKALSTK

Primary citation

Sequence differences between BAX and BAK core domains manifest as differences in their interactions with lipids. Miller, M.S., Cowan, A.D., Brouwer, J.M. et al. FEBS J (2024) 291:2335-2353. DOI 10.1111/febs.17031 · 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
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
7ADT 2.21 Å, Orf virus Apoptosis inhibitor ORFV125

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