8CZF: Human BAK

Human BAK in complex with the dF2 peptide. Determined by X-ray diffraction at 1.3 Å resolution. Released 11 Jan 2023.

Method: X-ray diffraction
Resolution: 1.3 Å
Organisms: Homo sapiens, synthetic construct
Chains: 2
Atoms: 1,630
Mol. weight: 21.61 kDa
Released: 11 Jan 2023

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

Secondary structure: helices and β-sheets

8CZF contains 11 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	21-23	3
α-helix	24-45	22
α-helix	55-57	3
α-helix	58-61	4
α-helix	70-100	31
α-helix	107-118	12
α-helix	125-144	20
α-helix	151-164	14
α-helix	167-173	7
α-helix	177-181	5

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-21	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bcl-2 homologous antagonist/killer	A	protein	170	Homo sapiens	Q16611 (AlphaFold model)
DF2 peptide	B	protein	24	synthetic construct

Sequence of entity 1 (A), FASTA

>8CZF_1 Bcl-2 homologous antagonist/killer (chains A)
GPLGSMSEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGR
QLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGY
RLALHVYQHGLTGFLGQVTRFVVDFMLHHSIARWIAQRGGWVAALNLGNG

Sequence of entity 2 (B), FASTA

>8CZF_2 DF2 peptide (chains B)
XSYIDKIADLIRKVAEEINSKLEX

Primary citation

Peptides from human BNIP5 and PXT1 and non-native binders of pro-apoptotic BAK can directly activate or inhibit BAK-mediated membrane permeabilization. Aguilar, F., Yu, S., Grant, R.A. et al. Structure (2023) 31:265-281.e7. DOI 10.1016/j.str.2023.01.001 · PubMed

Other PDB entries of the same protein (UniProt Q16611 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5VX1 1.22 Å, Bak L100A
8CZH 1.3 Å, Human BAK in complex with the dM2 peptide
2IMS 1.48 Å, The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site
2IMT 1.49 Å, The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site
9CPE 1.49 Å, Structural basis of BAK sequestration by MCL-1 and consequences for apoptosis initiation
5FMI 1.49 Å, Human Bak Q77L
7M5A 1.5 Å, Crystal Structure of human BAK in complex with W3W5_BID
5VWY 1.55 Å, Bak core latch dimer in complex with Bim-h3Pc-RT
5VX0 1.6 Å, Bak in complex with Bim-h3Glg
5VWZ 1.62 Å, Bak in complex with Bim-h3Pc
6UXQ 1.7 Å, Crystal structure of BAK core domain BH3-groove-dimer in complex with POPC and C8E4
8IGC 1.7 Å, Crystal structure of Bak bound to Bnip5 BH3

Browse structure collections

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