9P0D: Hemolysin

Crystal structure of Sr2+-bound RTX domain block V of adenylate cyclase toxin from Bordetella pertussis. Determined by X-ray diffraction at 1.5 Å resolution. Released 7 Jan 2026.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Bordetella pertussis
Chains
1
Atoms
1,297
Mol. weight
20.17 kDa
Ligands
SR, FOR
Released
7 Jan 2026

Explore 9P0D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9P0D contains 3 α-helices and 15 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: 3 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand1526-152831
β-strand1535-153732
β-strand1544-154631
β-strand1553-155532
β-strand1562-156431
β-strand1571-157332
β-strand1580-158451
β-strand1589-159352
β-strand1598-160361
β-strand1610-161452
α-helix1617-16193
β-strand1620-162561
β-strand1628-163361
β-strand1639-164241
α-helix1649-16513
β-strand1655-165732
β-strand1662-166432
α-helix1665-167511

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
HemolysinAprotein179Bordetella pertussisP0DKX7 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9P0D_1 Hemolysin (chains A)
MRGSHHHHHHGSHMELGASGSARDDVLIGDAGANVLNGLAGNDVLSGGAGDDVLLGDEGS
DLLSGDAGNDDLFGGQGDDTYLFGVGYGHDTIYESGGGHDTIRINAGADQLWFARQGNDL
EIRILGTDDALTVHDWYRDADHRVEIIHAANQAVDQAGIEKLVEAMAQYPDEFTSLEKN

Ligands and cofactors

IDNameFormulaCopies
SRStrontium ionSr8
FORFormyl groupC H2 O2

Water and common crystallization additives (CL, TRS, GOL, NA) are not listed.

Primary citation

Ion-selective conformational stabilization of a disordered repeats-in-toxin protein domain. Gudinas, A.P., Shambharkar, G.M., Chang, M.P. et al. Biophys J (2025) 124:4243-4254. DOI 10.1016/j.bpj.2025.10.014 · PubMed

Other PDB entries of the same protein (UniProt P0DKX7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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