3FDL: Bim BH3 peptide

Bim BH3 peptide in complex with Bcl-xL. Determined by X-ray diffraction at 1.78 Å resolution. Released 10 Mar 2009.

Method
X-ray diffraction
Resolution
1.78 Å
Organisms
Homo sapiens, synthetic construct
Chains
2
Atoms
1,594
Mol. weight
21.19 kDa
Released
10 Mar 2009

Explore 3FDL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3FDL contains 10 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: 9 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix-4-1923
α-helix26-10019
α-helix102-1109
α-helix119-13012
α-helix137-15620
α-helix161-17313
α-helix174-1785
α-helix179-1846
α-helix187-1937
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix87-10519

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Apoptosis regulator Bcl-XAprotein158Homo sapiensQ07817 (AlphaFold model)
Bcl-2-like protein 11Bprotein26synthetic constructO43521 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3FDL_1 Apoptosis regulator Bcl-X (chains A)
GPLGSMSQSNRELVVDFLSYKLSQKGYSWSQMAAVKQALREAGDEFELRYRRAFSDLTSQ
LHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMA
TYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER
Sequence of entity 2 (B), FASTA
>3FDL_2 Bcl-2-like protein 11 (chains B)
DMRPEIWIAQELRRIGDEFNAYYARR

Primary citation

High-Resolution Structural Characterization of a Helical alpha/beta-Peptide Foldamer Bound to the Anti-Apoptotic Protein Bcl-x(L). Lee, E.F., Sadowsky, J.D., Smith, B.J. et al. Angew Chem Int Ed Engl (2009) 48:4318-4322. DOI 10.1002/anie.200805761 · 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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