9SKU: PDB entry 9SKU

Cryo-EM structure of H. neapolitanus CsoSCA in reducing conditions, hexamer. Determined by electron microscopy at 2.06 Å resolution. Released 22 Apr 2026.

Method
Electron microscopy
Resolution
2.06 Å
Organisms
Escherichia coli K-12, Halothiobacillus neapolitanus c2
Chains
2
Atoms
7,740
Mol. weight
204.22 kDa
Ligands
ZN
Released
22 Apr 2026

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

Secondary structure: helices and β-sheets

9SKU contains 44 α-helices and 26 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: 21 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix56-7419
α-helix76-838
α-helix92-10413
α-helix110-1123
α-helix116-1194
α-helix123-14826
α-helix151-16212
β-strand165-17281
β-strand17312
α-helix176-1783
α-helix181-1855
β-strand19511
β-strand19912
α-helix206-22217
β-strand234-243101
α-helix254-2563
α-helix260-28021
β-strand289-29681
β-strand302-30761
β-strand313-32081
α-helix321-3288
α-helix333-34816
α-helix362-38625
α-helix392-3943
β-strand401-40553
β-strand417-42043
α-helix429-44214
α-helix444-4463
β-strand450-45893
α-helix465-48319
α-helix485-4895
β-strand493-50193
α-helix506-5072
β-strand508-51143
Chain B: 23 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix56-7419
α-helix76-838
α-helix92-10413
α-helix110-1123
α-helix116-1194
α-helix123-14220
α-helix146-1494
α-helix150-16213
β-strand165-17284
β-strand17315
α-helix176-1783
α-helix181-1855
α-helix190-1923
β-strand19514
β-strand19915
α-helix206-22217
β-strand234-243104
α-helix254-2563
α-helix260-28021
β-strand289-29684
β-strand302-30764
β-strand313-32084
α-helix321-3288
α-helix333-34816
α-helix362-38625
α-helix392-3943
β-strand401-40556
β-strand417-42046
α-helix429-44214
α-helix444-4463
β-strand450-45896
α-helix465-48319
α-helix485-4895
β-strand493-50196
α-helix506-5072
β-strand508-51146

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose/maltodextrin-binding periplasmic protein,Carboxysome shell carbonic anhydraseA, Bprotein919Escherichia coli K-12, Halothiobacillus neapolitanus c2O85042 (AlphaFold model), P0AEX9 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9SKU_1 Maltose/maltodextrin-binding periplasmic protein,Carboxysome shell carbonic anhydrase (chains A, B)
MWSHPQFEKGSSMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKF
PQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYP
IAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGY
AFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTIN
GPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTD
EGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAV
INAASGRQTVDEALKDAQTNSSSNNNNNNNNNNLGIEENLYFQSNANTRNTRSKQRAPFG
VSSSVKPRLDLIEQAPNPAYDRHPACITLPERTCRHPLTDLEANEQLGRCEDSVKNRFDR
VIPFLQVVAGIPLGLDYVTRVQELAQSSLGHTLPEELLKDNWISGHNLKGIFGYATAKAL
TAATEQFSRKIMSEKDDSASAIGFFLDCGFHAVDISPCADGRLKGLLPYILRLPLTAFTY
RKAYAGSMFDIEDDLAQWEKNELRRYREGVPNTADQPTRYLKIAVYHFSTSDPTHSGCAA
HGSNDRAALEAALTQLMKFREAVENAHCCGASIDILLIGVDTDTDAIRVHIPDSKGFLNP
YRYVDNTVTYAQTLHLAPDEARVIIHEAILNANRSDGWAKGNGVASEGMRRFIGQLLINN
LSQIDYVVNRHGGRYPPNDIGHAERYISVGDGFDEVQIRNLAYYAHLDTVEENAIDVDVG
IKIFTKLNLSRGLPIPIAIHYRYDPNVPGSRERTVVKARRIYNAIKERFSSLDEQNLLQF
RLSVQAQDIGSPIEEVASA

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Primary citation

Molecular mechanism of redox regulation of the alpha-carboxysomal carbonic anhydrase CsoSCA. Vogiatzi, N., Gaullier, G., Leufstadius, J. et al. bioRxiv (2026). DOI 10.64898/2026.04.02.716132

Other PDB entries of the same protein (UniProt O85042 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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