6MCY: Mouse Bak

Name: PDB 6MCY: Crystal structure of mouse Bak
Published: 2019-09-11
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: apoptosis

Crystal structure of mouse Bak. Determined by X-ray diffraction at 1.75 Å resolution. Released 11 Sept 2019.

Method: X-ray diffraction
Resolution: 1.75 Å
Organism: Mus musculus
Chains: 4
Atoms: 5,955
Mol. weight: 76.26 kDa
Released: 11 Sept 2019

Explore 6MCY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6MCY contains 47 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: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	20-48	29
α-helix	49-51	3
α-helix	53-54	2
α-helix	56-59	4
α-helix	68-83	16
α-helix	85-87	3
α-helix	88-95	8
α-helix	105-116	12
α-helix	123-142	20
α-helix	149-162	14
α-helix	165-171	7
α-helix	175-181	7

Chain B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	20-48	29
α-helix	49-51	3
α-helix	53-54	2
α-helix	56-59	4
α-helix	68-83	16
α-helix	84-87	4
α-helix	88-95	8
α-helix	105-117	13
α-helix	123-142	20
α-helix	149-162	14
α-helix	165-171	7
α-helix	175-180	6

Chain C: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	20-48	29
α-helix	49-51	3
α-helix	53-54	2
α-helix	56-58	3
α-helix	60-62	3
α-helix	68-83	16
α-helix	85-87	3
α-helix	88-96	9
α-helix	105-117	13
α-helix	123-142	20
α-helix	149-162	14
α-helix	165-171	7
α-helix	175-181	7

Chain D: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	20-48	29
α-helix	49-51	3
α-helix	53-54	2
α-helix	56-58	3
α-helix	68-95	28
α-helix	105-116	12
α-helix	123-142	20
α-helix	149-162	14
α-helix	165-171	7
α-helix	175-180	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bcl-2 homologous antagonist/killer	A, B, C, D	protein	169	Mus musculus	O08734 (AlphaFold model)

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

>6MCY_1 Bcl-2 homologous antagonist/killer (chains A, B, C, D)
GPLGSSEQQVAQDTEEVFRSYVFYLHQQEQETQGAAAPANPEMDNLPLEPNSILGQVGRQ
LALIGDDINRRYDTEFQNLLEQLQPTAGNAYELFTKIASSLFKSGISWGRVVALLGFGYR
LALYVYQRGLTGFLGQVTSFLADIILHHYIARWIAQRGGWVAALNFRRD

Primary citation

A small molecule interacts with VDAC2 to block mouse BAK-driven apoptosis. van Delft, M.F., Chappaz, S., Khakham, Y. et al. Nat Chem Biol (2019) 15:1057-1066. DOI 10.1038/s41589-019-0365-8 · PubMed

Other PDB entries of the same protein (UniProt O08734 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2VOH 1.9 Å, Structure of mouse A1 bound to the Bak BH3-domain
5FMJ 2.43 Å, Bcl-xL with mouse Bak BH3 Q75L complex
5KTG 2.8 Å, Crystal structure of mouse Bak BH3-in-groove homodimer (GFP)

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