5FMI: Human Bak Q77L

Human Bak Q77L. Determined by X-ray diffraction at 1.49 Å resolution. Released 1 Jun 2016.

Method: X-ray diffraction
Resolution: 1.49 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 1,442
Mol. weight: 18.5 kDa
Ligands: ZN
Released: 1 Jun 2016

Explore 5FMI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5FMI contains 11 α-helices and 0 β-strands across 1 chain. 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	24-50	27
α-helix	51-53	3
α-helix	55-56	2
α-helix	59-62	4
α-helix	70-82	13
α-helix	87-97	11
α-helix	104-118	15
α-helix	125-144	20
α-helix	151-164	14
α-helix	167-173	7
α-helix	177-183	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bcl-2 homologous antagonist/killer	A	protein	162	HOMO SAPIENS	Q16611 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5FMI_1 BCL-2 HOMOLOGOUS ANTAGONIST/KILLER (chains A)
SEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRLLAIIG
DDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYRLALHV
YQHGLTGFLGQVTRFVVDFMLHHSIARWIAQRGGWVAALNLG

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	3

Primary citation

Physiological Restraint of Bak by Bcl-Xl is Essential for Cell Survival. Lee, E.F., Grabow, S., Chappaz, S. et al. Genes Dev (2016) 30:1240. DOI 10.1101/GAD.279414.116 · 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
8CZF 1.3 Å, Human BAK in complex with the dF2 peptide
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
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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