8SPE: Apoptosis regulator BAX

Crystal structure of Bax core domain BH3-groove dimer - tetrameric fraction P31. Determined by X-ray diffraction at 2.3 Å resolution. Released 27 Dec 2023.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
36
Atoms
18,988
Mol. weight
324.07 kDa
Ligands
ZN
Released
27 Dec 2023

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

Secondary structure: helices and β-sheets

8SPE contains 146 α-helices and 0 β-strands across 36 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: 4 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix55-7218
α-helix74-818
α-helix88-9912
α-helix107-12115
Chain A: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix56-7116
α-helix74-807
α-helix88-9912
α-helix107-12115
Chain b: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix56-7116
α-helix74-818
α-helix88-9912
α-helix107-12317
Chain B: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix54-7219
α-helix74-829
α-helix88-9912
α-helix107-12216
Chain c: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix56-7116
α-helix74-807
α-helix88-9912
α-helix107-12216
Chain C: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix50-7122
α-helix74-807
α-helix88-9912
α-helix107-11812
α-helix119-1235
Chain d: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix55-7117
α-helix74-829
α-helix88-10013
α-helix107-12014
Chain D: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix56-7217
α-helix74-829
α-helix88-9912
α-helix107-12317

28 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apoptosis regulator BAXA, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, g, h, i, jprotein81Homo sapiensQ07812 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, g, h, i, j), FASTA
>8SPE_1 Apoptosis regulator BAX (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, g, h, i, j)
GPLGSDASTKKLSESLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNW
GRVVALFYFASKLVLKALSTK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn9

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

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:

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