5FMK: Bcl-xL with Bak BH3 complex

Bcl-xL with Bak BH3 complex. Determined by X-ray diffraction at 1.73 Å resolution. Released 1 Jun 2016.

Method
X-ray diffraction
Resolution
1.73 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
1,542
Mol. weight
22.14 kDa
Released
1 Jun 2016

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

Secondary structure: helices and β-sheets

5FMK contains 12 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: 11 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix59-7517
α-helix82-10524
α-helix108-1114
α-helix116-1183
α-helix119-13012
α-helix137-15620
α-helix161-17313
α-helix174-1785
α-helix179-1846
α-helix187-1959
α-helix199-2068
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix70-8516

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bcl-xlAprotein158HOMO SAPIENSQ07817 (AlphaFold model)
Bcl-2 homologous antagonist/killerBprotein34HOMO SAPIENSQ16611 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5FMK_1 BCL-XL (chains A)
GPLGSMSQSNRELVVDFLSYKLSQKGYSWSQMAAVKQALREAGDEFELRYRRAFSDLTSQ
LHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMA
TYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER
Sequence of entity 2 (B), FASTA
>5FMK_2 BCL-2 HOMOLOGOUS ANTAGONIST/KILLER (chains B)
LPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTM

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 Q07817 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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