9P0C: Hemolysin

Crystal structure of Ca2+-bound RTX domain block V of adenylate cyclase toxin from Bordetella pertussis. Determined by X-ray diffraction at 1.7 Å resolution. Released 7 Jan 2026.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Bordetella pertussis
Chains
2
Atoms
2,762
Mol. weight
39.14 kDa
Ligands
CA, ZN
Released
7 Jan 2026

Explore 9P0C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9P0C contains 7 α-helices and 32 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: 4 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand1514-151961
β-strand1522-152871
β-strand1535-153732
β-strand1542-154651
β-strand1553-155532
β-strand1561-156441
β-strand1571-157332
β-strand1580-158451
β-strand1589-159242
β-strand1598-160361
β-strand1610-161342
α-helix1617-16193
β-strand1620-162561
β-strand1628-163361
β-strand1639-164241
α-helix1649-16513
β-strand1655-165842
β-strand1661-166442
α-helix1665-167713
α-helix1679-16813
Chain B: 3 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand1517-151933
β-strand1522-152873
β-strand1535-153734
β-strand1542-154653
β-strand1553-155534
β-strand1562-156433
β-strand1571-157334
β-strand1580-158453
β-strand1589-159244
β-strand1598-160363
β-strand1610-161344
α-helix1617-16193
β-strand1620-162563
β-strand1628-163363
β-strand1639-164243
α-helix1649-16513
β-strand1655-165844
β-strand1662-166324
α-helix1665-167713

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
HemolysinA, Bprotein179Bordetella pertussisP0DKX7 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9P0C_1 Hemolysin (chains A, B)
MRGSHHHHHHGSHMELGASGSARDDVLIGDAGANVLNGLAGNDVLSGGAGDDVLLGDEGS
DLLSGDAGNDDLFGGQGDDTYLFGVGYGHDTIYESGGGHDTIRINAGADQLWFARQGNDL
EIRILGTDDALTVHDWYRDADHRVEIIHAANQAVDQAGIEKLVEAMAQYPDEFTSLEKN

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa16
ZNZinc ionZn4

Water and common crystallization additives (CL, GOL) 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:

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