9KTM: Alpha-hemolysin heptameric pre-pore state

Alpha-hemolysin heptameric pre-pore state bound to 10:PC lipid chains derived from 10:0 PC liposomes. Determined by electron microscopy at 2.9 Å resolution. Released 11 Jun 2025.

Method
Electron microscopy
Resolution
2.9 Å
Organism
Staphylococcus aureus
Chains
7
Atoms
14,084
Mol. weight
237 kDa
Ligands
P1O
Released
11 Jun 2025

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

Secondary structure: helices and β-sheets

9KTM contains 28 α-helices and 175 β-strands across 7 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.

Chains A, B, C, D, E, F and G: 4 helices, 25 β-strands

ElementResiduesLengthSheet
α-helix3-53
β-strand22112
β-strand24113
β-strand27-28214
β-strand34-36314
β-strand39113
β-strand4811
β-strand53-56415
β-strand59-61314
β-strand66-69416
β-strand77-79316
β-strand80-87817
β-strand97-100415
α-helix1041
β-strand155-158417
β-strand166-170517
α-helix206-2083
α-helix218-2225
β-strand224114
β-strand229-233515
β-strand248118
β-strand250-254517
β-strand256-257219
β-strand260120
β-strand265120
β-strand268-269219
β-strand279118
β-strand284-285221
β-strand290-291221

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-hemolysinA, B, C, D, E, F, Gprotein293Staphylococcus aureusQ2G1X0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>9KTM_1 Alpha-hemolysin (chains A, B, C, D, E, F, G)
ADSDINIKTGTTDIGSNTTVKTGDLVTYDKENGMHKKVFYSFIDDKNHNKKLLVIRTKGT
IAGQYRVYSEEGANKSGLAWPSAFKVQLQLPDNEVAQISDYYPRNSIDTKEYMSTLTYGF
NGNVTGDDTGKIGGLIGANVSIGHTLKYVQPDFKTILESPTDKKVGWKVIFNNMVNQNWG
PYDRDSWNPVYGNQLFMKTRNGSMKAADNFLDPNKASSLLSSGFSPDFATVITMDRKASK
QQTNIDVIYERVRDDYQLHWTSTNWKGTNTKDKWTDRSSERYKIDWEKEEMTN

Ligands and cofactors

IDNameFormulaCopies
P1O1,2-didecanoyl-sn-glycero-3-phosphocholineC28 H57 N O8 P7

Primary citation

Structural insights into pre-pore intermediates of alpha-hemolysin in the lipidic environment. Chatterjee, A., Roy, A., Satheesh, T. et al. Nat Commun (2025) 16:6348-6348. DOI 10.1038/s41467-025-61741-x · PubMed

Other PDB entries of the same protein (UniProt Q2G1X0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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