8DO1: Human Sec61 complex inhibited by ipomoeassin F

Cryo-EM structure of the human Sec61 complex inhibited by ipomoeassin F. Determined by electron microscopy at 3.01 Å resolution. Released 24 May 2023.

Method
Electron microscopy
Resolution
3.01 Å
Organism
Homo sapiens
Chains
3
Atoms
4,339
Mol. weight
70.77 kDa
Ligands
SXF
Released
24 May 2023

Explore 8DO1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8DO1 contains 27 α-helices and 11 β-strands across 3 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: 24 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix5-139
β-strand18-1921
α-helix20-223
α-helix25-273
α-helix28-4518
β-strand4912
α-helix501
α-helix59-602
β-strand7512
α-helix82-9615
α-helix106-13328
α-helix140-1434
α-helix145-16824
α-helix169-1735
α-helix178-19619
β-strand20013
β-strand20913
α-helix212-22312
α-helix227-2348
α-helix242-25918
β-strand262-26984
β-strand277-28264
α-helix289-31123
α-helix316-3216
β-strand323-32425
β-strand337-33935
α-helix341-3444
α-helix351-3566
α-helix358-38225
α-helix387-39711
β-strand399-40134
α-helix410-4145
α-helix417-43822
α-helix443-46725
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix8-2417
α-helix30-6536
Chain C: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand67-6821
α-helix71-9525

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein transport protein Sec61 subunit alpha isoform 1Aprotein476Homo sapiensP61619 (AlphaFold model)
Protein transport protein Sec61 subunit gammaBprotein68Homo sapiensP60059 (AlphaFold model)
Protein transport protein Sec61 subunit betaCprotein96Homo sapiensP60468 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8DO1_1 Protein transport protein Sec61 subunit alpha isoform 1 (chains A)
MAIKFLEVIKPFCVILPEIQKPERKIQFKEKVLWTAITLFIFLVCCQIPLFGIMSSDSAD
PFYWMRVILASNRGTLMELGISPIVTSGLIMQLLAGAKIIEVGDTPKDRALFNGAQKLFG
MIITIGQSIVYVMTGMYGDPSEMGAGICLLITIQLFVAGLIVLLLDELLQKGYGLGSGIS
LFIATNICETIVWKAFSPTTVNTGRGMEFEGAIIALFHLLATRTDKVRALREAFYRQNLP
NLMNLIATIFVFAVVIYFQGFRYELPIRSTKVRGQIGIYPIKLFYTSNIPIILQSALVSN
LYVISQMLSARFSGNLLVSLLGTWSDTSSGGPARAYPVGGLCYYLSPPESFGSVLEDPVH
AVVYIVFMLGSCAFFSKTWIEVSGSSPRDIAKQFKDQGMVINGKRETSIYRELKKIIPTA
AAFGGLCIGALSVLADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEVGSMGALLF
Sequence of entity 2 (B), FASTA
>8DO1_2 Protein transport protein Sec61 subunit gamma (chains B)
MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIP
INNIIVGG
Sequence of entity 3 (C), FASTA
>8DO1_3 Protein transport protein Sec61 subunit beta (chains C)
MPGPTPSGTNVGSSGRSPSKAVAARAAGSTVRQRKNASCGTRSAGRTTSAGTGGMWRFYT
EDSPGLKVGPVPVLVMSLLFIASVFMLHIWGKYTRS

Ligands and cofactors

IDNameFormulaCopies
SXF[(1~{S},3~{R},4~{S},5~{R},6~{R},8~{R},10~{S},23~{R},24~{R},25~{R},26~{R})-5-ace…C44 H62 O151

Primary citation

A common mechanism of Sec61 translocon inhibition by small molecules. Itskanov, S., Wang, L., Junne, T. et al. Nat Chem Biol (2023) 19:1063-1071. DOI 10.1038/s41589-023-01337-y · PubMed

Other PDB entries of the same protein (UniProt P61619 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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