5UUL: Human Bfl-1

Human Bfl-1 in complex with PUMA BH3. Determined by X-ray diffraction at 1.33 Å resolution. Released 21 Jun 2017.

Method: X-ray diffraction
Resolution: 1.33 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,651
Mol. weight: 20.36 kDa
Released: 21 Jun 2017

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

Secondary structure: helices and β-sheets

5UUL 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

Element	Residues	Length
α-helix	6-21	16
α-helix	23-26	4
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	139-144	6
α-helix	145-148	4

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-19	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bcl-2-related protein A1	A	protein	152	Homo sapiens	Q16548 (AlphaFold model)
Bcl-2-binding component 3	B	protein	25	Homo sapiens	Q9BXH1 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5UUL_1 Bcl-2-related protein A1 (chains A)
GMTDCEFGYIYRLAQDYLQCVLQIPQPGSGPSKTSRVLQNVAFSVQKEVEKNLKSCLDNV
NVVSVDTARTLFNQVMEKEFEDGIINWGRIVTIFAFEGILIKKLLRQQIAPDVDTYKEIS
YFVAEFIMNNTGEWIRQNGGWENGFVKKFEPK

Sequence of entity 2 (B), FASTA

>5UUL_2 Bcl-2-binding component 3 (chains B)
XQWAREIGAQLRRMADDLNAQYERX

Primary citation

Epistatic mutations in PUMA BH3 drive an alternate binding mode to potently and selectively inhibit anti-apoptotic Bfl-1. Jenson, J.M., Ryan, J.A., Grant, R.A. et al. Elife (2017) 6. DOI 10.7554/eLife.25541 · 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
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
6MBB 1.59 Å, Human Bfl-1 in complex with the designed peptide dF1

Browse structure collections

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