9FKZ: Bcl-2-related protein A1

Discovery of a Series of Covalent, Cell Active Bfl-1 Inhibitors. Determined by X-ray diffraction at 1.68 Å resolution. Released 2 Oct 2024.

Method
X-ray diffraction
Resolution
1.68 Å
Organism
Homo sapiens
Chains
1
Atoms
1,286
Mol. weight
17.81 kDa
Ligands
A1IDO
Released
2 Oct 2024

Explore 9FKZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9FKZ contains 10 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: 10 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix6-2116
α-helix24-252
α-helix32-5120
α-helix53-564
α-helix64-7815
α-helix86-10621
α-helix112-1143
α-helix115-13622
α-helix140-1445
α-helix145-1484

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bcl-2-related protein A1Aprotein152Homo sapiensQ16548 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9FKZ_1 Bcl-2-related protein A1 (chains A)
GMTDCEFGYIYRLAQDYLQCVLQIPQPGSGPSKTSRVLQNVAFSVQKEVEKNLKSCLDNV
NVVSVDTARTLFNQVMEKEFEDGIINWGRIVTIFAFEGILIKKLLRQQIAPDVDTYKEIS
YFVAEFIMNNTGEWIRQNGGWENGFVKKFEPK

Ligands and cofactors

IDNameFormulaCopies
A1IDO~{N}-[4-[(1~{R},3~{R})-3-azanylcyclopentyl]oxyphenyl]-~{N}-[(4-chlorophenyl)met…C21 H23 Cl N2 O21

Primary citation

Structure-Based Optimization of a Series of Covalent, Cell Active Bfl-1 Inhibitors. Lucas, S.C.C., Blackwell, J.H., Borjesson, U. et al. J Med Chem (2024) 67:16455-16479. DOI 10.1021/acs.jmedchem.4c01288 · PubMed

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

Browse structure collections

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