5Z3U: Transcription regulatory protein SNF2

Structure of Snf2-nucleosome complex at shl2 in ADP BeFx state. Determined by electron microscopy at 4.31 Å resolution. Released 22 May 2019.

Method
Electron microscopy
Resolution
4.31 Å
Organisms
Saccharomyces cerevisiae, Xenopus laevis, synthetic construct
Chains
11
Atoms
16,766
Mol. weight
297.57 kDa
Ligands
ADP, MG, BEF
Released
22 May 2019

Explore 5Z3U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5Z3U contains 74 α-helices and 34 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.

Chains A and E: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix41-422
α-helix45-5612
α-helix64-7613
β-strand83-8426
α-helix86-11328
β-strand118-11927
α-helix121-13111
Chain B: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix26-283
α-helix31-4111
β-strand45-4627
α-helix50-7627
β-strand80-8126
α-helix83-9311
β-strand9718
Chain C: 5 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix17-215
α-helix27-3610
β-strand42-4329
α-helix47-7226
β-strand77-78210
α-helix80-8910
α-helix91-977
β-strand100-101211
Chains D and H: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix35-439
β-strand50-51210
α-helix53-8028
β-strand85-8629
α-helix88-9811
α-helix102-12019
Chain F: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix25-284
α-helix31-4010
β-strand45-46213
α-helix50-7526
β-strand80-81212
α-helix83-9311
β-strand96-97211
Chain G: 5 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix17-215
α-helix27-3610
β-strand42-43214
α-helix47-7226
β-strand77-78215
α-helix80-8910
α-helix91-977
β-strand10118
Chain O: 38 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix675-6839
α-helix684-6896
α-helix744-7474
α-helix758-7592
α-helix770-78314
β-strand789-79021
α-helix798-81215
β-strand819-82352
α-helix829-8379
α-helix853-8608
α-helix861-8633
β-strand868-87252
α-helix875-8784
α-helix880-8834
β-strand888-89033
β-strand892-89322
α-helix896-8983
α-helix905-9139
β-strand916-91833
β-strand921-92221
α-helix934-9418
α-helix949-9524
α-helix953-9564
α-helix968-9714
α-helix972-9798
α-helix980-9878
α-helix996-9994
β-strand101314
α-helix1017-10259
α-helix1051-106010
α-helix1066-10672
α-helix1068-10725
α-helix1087-110216
β-strand1106-111055
α-helix1115-112612
β-strand1130-113235
α-helix1141-115010
β-strand1158-116255
β-strand1177-118045
α-helix1187-11948
β-strand1208-121035
β-strand121314
α-helix1217-123317
α-helix1236-12394
α-helix1249-12524
α-helix1253-12575
α-helix1258-126811
α-helix1280-12878
α-helix1291-12966
α-helix1298-13003
α-helix1302-13065
α-helix1337-134610

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcription regulatory protein SNF2Oprotein735Saccharomyces cerevisiaeP22082 (AlphaFold model)
Histone H3.2A, Eprotein135Xenopus laevisP84233 (AlphaFold model)
Histone H4B, Fprotein102Xenopus laevisP62799 (AlphaFold model)
Histone H2AC, Gprotein129Xenopus laevisQ6AZJ8 (AlphaFold model)
Histone H2B 1.1D, Hprotein122Xenopus laevisP02281
DNA (167-mer)IDNA167synthetic construct
DNA (167-mer)JDNA167synthetic construct
Sequence of entity 1 (O), FASTA
>5Z3U_1 Transcription regulatory protein SNF2 (chains O)
AYIKLLDQTKDTRITHLLRQTNAFLDSLTRAVKDQQKYTKEMIDSHIKEASEEVDDLSMV
PKMKDEEYDDDDDNSNVDYYNVAHRIKEDIKKQPSILVGGTLKDYQIKGLQWMVSLFNNH
LNGILADEMGLGKTIQTISLLTYLYEMKNIRGPYLVIVPLSTLSNWSSEFAKWAPTLRTI
SFKGSPNERKAKQAKIRAGEFDVVLTTFEYIIKERALLSKVKWVHMIIDEGHRMKNAQSK
LSLTLNTHYHADYRLILTGTPLQNNLPELWALLNFVLPKIFNSVKSFDEWFNTPFANTGG
QDKIELSEEETLLVIRRLHKVLRPFLLRRLKKDVEKELPDKVEKVVKCKMSALQQIMYQQ
MLKYRRLFIGDQNNKKMVGLRGFNNQIMQLKKICNHPFVFEEVEDQINPTRETNDDIWRV
AGKFELLDRILPKLKATGHRVLIFFQMTQIMDIMEDFLRYINIKYLRLDGHTKSDERSEL
LRLFNAPDSEYLCFILSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQKNE
VRILRLITTNSVEEVILERAYKKLDIDGKVIQAGKFDNKSTSEEQEALLRSLLDAEEERR
KKRESGVEEEEELKDSEINEILARNDEEMAVLTRMDEDRSKKEEELGVKSRLLEKSELPD
IYSRDIGAELKREESESAAVYNGRGARERKTATYNDNMSEEQWLRQFEVSDDEKNDKQAR
KQRTKKEDKSEAIDG
Sequence of entity 2 (A, E), FASTA
>5Z3U_2 Histone H3.2 (chains A, E)
ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 3 (B, F), FASTA
>5Z3U_3 Histone H4 (chains B, F)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 4 (C, G), FASTA
>5Z3U_4 Histone H2A (chains C, G)
SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT
ESSKSAKSK
Sequence of entity 5 (D, H), FASTA
>5Z3U_5 Histone H2B 1.1 (chains D, H)
AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMN
SFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTS
AK
Sequence of entity 6 (I), FASTA
>5Z3U_6 DNA (167-MER) (chains I)
ATCGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAA
ACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCA
GGCACGTGTCAGATATATACATCCTGAAGCTTGTCGAGAAGTACGAT
Sequence of entity 7 (J), FASTA
>5Z3U_7 DNA (167-MER) (chains J)
ATCGTACTTCTCGACAAGCTTCAGGATGTATATATCTGACACGTGCCTGGAGACTAGGGA
GTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTA
GAGCTGTCTACGACCAATTGAGCGGCCTCGGCACCGGGATTCTCGAT

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21
MGMagnesium ionMg1
BEFBeryllium trifluoride ionBe F31

Primary citation

Mechanism of DNA translocation underlying chromatin remodelling by Snf2. Li, M., Xia, X., Tian, Y. et al. Nature (2019) 567:409-413. DOI 10.1038/s41586-019-1029-2 · PubMed

Other PDB entries of the same protein (UniProt P22082 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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