6MBB: Human Bfl-1

Human Bfl-1 in complex with the designed peptide dF1. Determined by X-ray diffraction at 1.59 Å resolution. Released 6 Mar 2019.

Method: X-ray diffraction
Resolution: 1.59 Å
Organisms: Homo sapiens, synthetic construct
Chains: 2
Atoms: 1,584
Mol. weight: 19.97 kDa
Released: 6 Mar 2019

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

Secondary structure: helices and β-sheets

6MBB 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

Element	Residues	Length
α-helix	1-4	4
α-helix	6-20	15
α-helix	24-25	2
α-helix	32-51	20
α-helix	53-57	5
α-helix	64-78	15
α-helix	86-106	21
α-helix	114-136	23
α-helix	139	1
α-helix	140-144	5
α-helix	145-148	4

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-21	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bcl-2-related protein A1	A	protein	152	Homo sapiens	Q16548 (AlphaFold model)
dF1	B	protein	24	synthetic construct

Sequence of entity 1 (A), FASTA

>6MBB_1 Bcl-2-related protein A1 (chains A)
GMTDCEFGYIYRLAQDYLQCVLQIPQPGSGPSKTSRVLQNVAFSVQKEVEKNLKSCLDNV
NVVSVDTARTLFNQVMEKEFEDGIINWGRIVTIFAFEGILIKKLLRQQIAPDVDTYKEIS
YFVAEFIMNNTGEWIRQNGGWENGFVKKFEPK

Sequence of entity 2 (B), FASTA

>6MBB_2 dF1 (chains B)
XSYVDKIADVMREVAEKINSDLTX

Primary citation

Tertiary Structural Motif Sequence Statistics Enable Facile Prediction and Design of Peptides that Bind Anti-apoptotic Bfl-1 and Mcl-1. Frappier, V., Jenson, J.M., Zhou, J. et al. Structure (2019) 27:606-617.e5. DOI 10.1016/j.str.2019.01.008 · PubMed

Other PDB entries of the same protein (UniProt Q16548 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9GIR 1.07 Å, BFL1 covalently bound to inhibitor compound 39
9GIT 1.15 Å, BFL1 covalently bound to inhibitor compound 43
5UUK 1.2 Å, Human Bfl-1 in complex with a Bfl-1-specific selected peptide
5UUL 1.33 Å, Human Bfl-1 in complex with PUMA BH3
9GIS 1.39 Å, BFL1 covalently bound to inhibitor compound 17
9GIQ 1.42 Å, BFL1 covalently bound to inhibitor compound 13
9S6M 1.43 Å, Structure of BFL1 in complex with a covalent inhibitor, alternative series, cmpd25
9GIP 1.46 Å, BFL1 covalently bound to inhibitor compound 7
6E3I 1.48 Å, Human Bfl-1 in complex with the Bfl-1-specific designed peptide srt.F4
6E3J 1.48 Å, Human Bfl-1 in complex with the Bfl-1-specific designed peptide srt.F10
9EW8 1.49 Å, Discovery of a Series of Covalent, Cell Active Bfl-1 Inhibitors
9FKY 1.56 Å, Discovery of a Series of Covalent, Cell Active Bfl-1 Inhibitors

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