8SWI: Eukaryotic huntingtin interacting protein B

Crystal structure of legAS4 from Legionella pneumophila subsp. pneumophila with histone H3 (1-12)peptide. Determined by X-ray diffraction at 3.0 Å resolution. Released 27 Dec 2023.

Method
X-ray diffraction
Resolution
3.0 Å
Organisms
Legionella pneumophila subsp. pneumophila, Homo sapiens
Chains
2
Atoms
3,647
Mol. weight
53.61 kDa
Ligands
SAH
Released
27 Dec 2023

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

Secondary structure: helices and β-sheets

8SWI contains 28 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: 28 helices, 25 β-strands

ElementResiduesLengthSheet
α-helix83-864
α-helix89-957
β-strand10611
β-strand117-12152
α-helix123-1253
β-strand131-13552
β-strand13913
β-strand144-14744
β-strand151-15445
α-helix155-16410
α-helix170-1723
β-strand173-17645
β-strand179-18245
β-strand18711
α-helix189-1924
β-strand194-19524
β-strand202-20984
β-strand212-21984
α-helix2221
β-strand22313
α-helix2241
α-helix2271
β-strand22812
α-helix2291
β-strand230-23124
α-helix238-2436
α-helix256-2627
α-helix264-2663
β-strand267-27156
β-strand27617
α-helix277-2793
β-strand28117
β-strand286-29056
α-helix291-2977
β-strand318-31926
β-strand32018
β-strand32618
α-helix337-3448
α-helix347-3559
α-helix371-38111
α-helix386-39712
β-strand40519
β-strand41119
α-helix412-4198
α-helix422-43514
α-helix441-4433
β-strand446110
α-helix454-4607
α-helix464-47310
α-helix477-4815
α-helix487-50014
α-helix506-51813
α-helix525-5306
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand3110

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Eukaryotic huntingtin interacting protein BAprotein451Legionella pneumophila subsp. pneumophilaQ5ZUS4 (AlphaFold model)
Histone H3 peptidedBprotein12Homo sapiensP68431 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8SWI_1 Eukaryotic huntingtin interacting protein B (chains A)
NADEWIDTSKIMLDLHIDNMSSSDYIPSAIDRTDLVMVQSVHLLRKTGGRGLFAREDIPK
GTCIGIYTGEVYSEQEFEQYLKEHVGSDKSYAMYVGGRVIDAARKGNLTRYINFSDSQDN
AEFVETTLNRKKVAKVITTKNIKAGQQLLINYNTYEEQASRYYYFLNPGDGWLSAQEFYQ
TYQSQYRLEQMPYNLEGFDLKAGDRVLMTQIGRIILANYSLAKEQELNASDIDLPFLKVG
SDEKILDFDEADTFTPLMAACYLGQVENVKWLIEHGANIDQQQSHSGHCPLSLTLKGYSL
AKDTQKYIDIIQLLIKNQVNLLVHDRSDKTFLHNAALVLNNLDFQSVVKFLIGQNPIDIN
EYFTYIDENDFDIVMHCYNNKLFDKALVLLAFYPDYFKRNYMSDNEGHNQFNINAFRKAI
KDFNSNERSILLMQLRESGLHLPEDLLEQLG
Sequence of entity 2 (B), FASTA
>8SWI_2 Histone H3 peptided (chains B)
ARTKQTARKSTG

Ligands and cofactors

IDNameFormulaCopies
SAHS-adenosyl-L-homocysteineC14 H20 N6 O5 S1

Primary citation

The SET and ankyrin domains of the secreted Legionella pneumophila histone methyltransferase work together to modify host chromatin. Rolando, M., Wah Chung, I.Y., Xu, C. et al. mBio (2023) 14:e0165523-e0165523. DOI 10.1128/mbio.01655-23 · PubMed

Other PDB entries of the same protein (UniProt Q5ZUS4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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