9P6C: Hemolysin

RTX domain block V of adenylate cyclase toxin with mutations D1533N, A1542N, D1560N, S1569N, D1587N, H1598N, H1608N. Determined by X-ray diffraction at 1.99 Å resolution. Released 24 Dec 2025.

Method
X-ray diffraction
Resolution
1.99 Å
Organism
Bordetella pertussis
Chains
2
Atoms
2,331
Mol. weight
38.92 kDa
Ligands
CA
Released
24 Dec 2025

Explore 9P6C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9P6C contains 5 α-helices and 30 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: 3 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand1527-152821
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-helix1665-167713
Chain B: 2 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand1527-152823
β-strand1535-153734
β-strand1544-154633
β-strand1553-155534
β-strand1562-156433
β-strand1571-157334
β-strand1580-158453
β-strand1589-159354
β-strand1598-160363
β-strand1610-161454
β-strand1620-162563
β-strand1628-163363
β-strand1639-164243
α-helix1649-16513
β-strand1655-165844
β-strand1662-166434
α-helix1665-16739

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
HemolysinA, Bprotein180Bordetella pertussisP0DKX7 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9P6C_1 Hemolysin (chains A, B)
MRGSHHHHHHGSHMELGASGSARNDVLIGDAGNNVLNGLAGNDVLSGGAGNDVLLGDEGN
DLLSGDAGNDDLFGGQGNDTYLFGVGYGNDTIYESGGGNDTIRINAGADQLWFARQGNDL
EIRILGTDDALTVHDWYRDADHRVEIIHAANQAVDQAGIEKLVEAMAQYPDEFTSLEKLN

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa16

Primary citation

Repetitive proteins that undergo large conformational changes evade structural prediction algorithms. Chang, M.P., Jin, T., Gudinas, A.P. et al. J Chem Phys (2025) 163. DOI 10.1063/5.0304777 · 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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