9JNT: Isw1-nucleosome complex in ADP* state

Structure of isw1-nucleosome complex in ADP* state. Determined by electron microscopy at 2.7 Å resolution. Released 9 Apr 2025.

Method
Electron microscopy
Resolution
2.7 Å
Organisms
Xenopus laevis, Escherichia coli K-12, Saccharomyces cerevisiae S288C
Chains
11
Atoms
16,283
Mol. weight
321.89 kDa
Ligands
ADP, MG
Released
9 Apr 2025

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

Secondary structure: helices and β-sheets

9JNT contains 67 α-helices and 36 β-strands across 9 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: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix41-422
α-helix45-5410
α-helix64-7512
β-strand83-8421
α-helix86-11328
β-strand118-11922
α-helix121-13111
Chain B: 3 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix31-4111
β-strand45-4622
α-helix50-7526
β-strand80-8121
α-helix83-9311
β-strand97-9823
Chain C: 5 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix17-215
α-helix27-3610
β-strand42-4324
α-helix46-7227
β-strand77-7825
α-helix80-8910
α-helix91-966
β-strand101-10226
Chain D: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix35-4511
β-strand50-5125
α-helix53-8028
β-strand85-8624
α-helix88-9811
α-helix102-11918
Chain E: 6 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix41-422
α-helix45-5410
α-helix64-7411
α-helix75-773
β-strand83-8427
α-helix86-11328
β-strand118-11928
α-helix121-13111
Chain F: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix26-283
α-helix31-4111
β-strand45-4628
α-helix50-7526
β-strand80-8127
α-helix83-9311
β-strand97-9826
Chain G: 6 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix17-204
α-helix27-3610
β-strand42-4329
α-helix47-7226
β-strand77-78210
α-helix80-878
α-helix91-966
β-strand101-10223
α-helix113-1153
Chain H: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix35-4511
β-strand50-51210
α-helix53-8028
β-strand85-8629
α-helix88-9811
α-helix102-12019

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone H3A, Eprotein135Xenopus laevisA0A310TTQ1 (AlphaFold model)
Histone H4B, Fprotein102Xenopus laevisA0A8J1LTD2 (AlphaFold model)
Histone H2AC, Gprotein129Xenopus laevisP06897 (AlphaFold model)
Histone H2BD, Hprotein122Xenopus laevisP02281 (AlphaFold model)
DNA (146-mer)IDNA146Escherichia coli K-12
DNA (146-mer)JDNA146Escherichia coli K-12
ISWI chromatin-remodeling complex ATPase ISW1Kprotein1061Saccharomyces cerevisiae S288CP38144
Sequence of entity 1 (A, E), FASTA
>9JNT_1 Histone H3 (chains A, E)
ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 2 (B, F), FASTA
>9JNT_2 Histone H4 (chains B, F)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 3 (C, G), FASTA
>9JNT_3 Histone H2A (chains C, G)
SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT
ESSKSAKSK
Sequence of entity 4 (D, H), FASTA
>9JNT_4 Histone H2B (chains D, H)
AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMN
SFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTS
AK
Sequence of entity 5 (I), FASTA
>9JNT_5 DNA (146-MER) (chains I)
TCGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAA
CGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAG
GCACGTGTCAGATATATACATCCGAT
Sequence of entity 6 (J), FASTA
>9JNT_6 DNA (146-MER) (chains J)
ATCGGATGTATATATCTGACACGTGCCTGGAGACTAGGGAGTAATCCCCTTGGCGGTTAA
AACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGTCTACGACCAATTG
AGCGGCCTCGGCACCGGGATTCTCGA
Sequence of entity 7 (K), FASTA
>9JNT_7 ISWI chromatin-remodeling complex ATPase ISW1 (chains K)
ENLKPFQVGLPPHDPESNKKRYLLKDANGKKFDLEGTTKRFEHLLSLSGLFKHFIESKAA
KDPKFRQVLDVLEENKANGKGKGKHQDVRRRKTEHEEDAELLKEEDSDDDESIEFQFRES
PAYVNGQLRPYQIQGVNWLVSLHKNKIAGILADEMGLGKTLQTISFLGYLRYIEKIPGPF
LVIAPKSTLNNWLREINRWTPDVNAFILQGDKEERAELIQKKLLGCDFDVVIASYEIIIR
EKSPLKKINWEYIIIDEAHRIKNEESMLSQVLREFTSRNRLLITGTPLQNNLHELWALLN
FLLPDIFSDAQDFDDWFSSESTEEDQDKIVKQLHTVLQPFLLRRIKSDVETSLLPKKELN
LYVGMSSMQKKWYKKILEKDLDAVNGSNGSKESKTRLLNIMMQLRKCCNHPYLFDGAEPG
PPYTTDEHLVYNAAKLQVLDKLLKKLKEEGSRVLIFSQMSRLLDILEDYCYFRNYEYCRI
DGSTAHEDRIQAIDDYNAPDSKKFVFLLTTRAGGLGINLTSADVVVLYDSDWNPQADLQA
MDRAHRIGQKKQVKVFRLVTDNSVEEKILERATQKLRLDQLVIQQNRTSLKKKENKADSK
DALLSMIQHGAADVFKSGTSTGSAGTPEPGSGEKGDDIDLDELLLKSENKTKSLNAKYET
LGLDDLQKFNQDSAYEWNGQDFKKKIQRDIISPLLLNPTKRERKENYSIDNYYKDVLNTG
RSSTPSHPRMPKPHVFHSHQLQPPQLKVLYEKERMWTAKKTGYVPTMDDVKAAYGDISDE
EEKKQKLELLKLSVNNSQPLTEEEEKMKADWESEGFTNWNKLEFRKFITVSGKYGRNSIQ
AIARELAPGKTLEEVRAYAKAFWSNIERIEDYEKYLKIIENEEEKIKRVKMQQEALRRKL
SEYKNPFFDLKLKHPPSSNNKRTYSEEEDRFILLMLFKYGLDRDDVYELVRDEIRDCPLF
ELDFYFRSRTPVELARRGNTLLQCLEKEFNAGIVLDDATKDRMKKEDENGKRIREEFADQ
TANEKENVDGVESKKAKIEDTSNVGTEQLVAEKIPENETTH

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21
MGMagnesium ionMg1

Primary citation

Structural insights into chromatin remodeling by ISWI during active ATP hydrolysis. Sia, Y., Pan, H., Chen, K. et al. Science (2025) 388:eadu5654-eadu5654. DOI 10.1126/science.adu5654 · PubMed

Other PDB entries of the same protein (UniProt A0A310TTQ1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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