Complex of Snf2-Nucleosome complex with Snf2 bound to position +6 of the nucleosome. Determined by electron microscopy at 3.97 Å resolution. Released 19 Apr 2017.
Explore 5X0X in 3D Show helices and sheets RCSB PDB PDBe
5X0X contains 73 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-42 | 2 | |
| α-helix | 45-54 | 10 | |
| α-helix | 64-78 | 15 | |
| β-strand | 83-84 | 2 | 1 |
| α-helix | 86-113 | 28 | |
| β-strand | 118 | 1 | 2 |
| α-helix | 121-131 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-28 | 4 | |
| α-helix | 31-41 | 11 | |
| β-strand | 45 | 1 | 2 |
| α-helix | 50-76 | 27 | |
| β-strand | 80-81 | 2 | 1 |
| α-helix | 83-93 | 11 | |
| β-strand | 96-98 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-20 | 4 | |
| α-helix | 27-36 | 10 | |
| β-strand | 42-43 | 2 | 4 |
| α-helix | 46-72 | 27 | |
| β-strand | 77-78 | 2 | 5 |
| α-helix | 80-89 | 10 | |
| α-helix | 92-97 | 6 | |
| β-strand | 100-102 | 3 | 6 |
| α-helix | 113-115 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 35-45 | 11 | |
| β-strand | 50-51 | 2 | 5 |
| α-helix | 53-80 | 28 | |
| β-strand | 85-86 | 2 | 4 |
| α-helix | 88-98 | 11 | |
| α-helix | 101-120 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 671-688 | 18 | |
| α-helix | 744-748 | 5 | |
| α-helix | 769-783 | 15 | |
| β-strand | 788 | 1 | 11 |
| β-strand | 789-790 | 2 | 12 |
| α-helix | 792-793 | 2 | |
| α-helix | 798-810 | 13 | |
| β-strand | 819-823 | 5 | 11 |
| α-helix | 825-837 | 13 | |
| β-strand | 844-845 | 2 | 11 |
| α-helix | 850-862 | 13 | |
| β-strand | 868-872 | 5 | 11 |
| α-helix | 874-878 | 5 | |
| α-helix | 880-885 | 6 | |
| β-strand | 888-892 | 5 | 11 |
| α-helix | 896-900 | 5 | |
| α-helix | 905-912 | 8 | |
| β-strand | 916-920 | 5 | 11 |
| α-helix | 933-934 | 2 | |
| α-helix | 935-939 | 5 | |
| α-helix | 940-941 | 2 | |
| α-helix | 943-947 | 5 | |
| α-helix | 949-957 | 9 | |
| α-helix | 968 | 1 | |
| α-helix | 969-973 | 5 | |
| α-helix | 976-987 | 12 | |
| β-strand | 991-992 | 2 | 12 |
| β-strand | 1009-1011 | 3 | 13 |
| β-strand | 1014 | 1 | 14 |
| α-helix | 1015-1016 | 2 | |
| α-helix | 1017-1021 | 5 | |
| α-helix | 1026-1029 | 4 | |
| α-helix | 1049-1060 | 12 | |
| α-helix | 1067-1072 | 6 | |
| α-helix | 1087-1102 | 16 | |
| α-helix | 1104-1105 | 2 | |
| β-strand | 1106-1108 | 3 | 13 |
| α-helix | 1115-1126 | 12 | |
| β-strand | 1130-1132 | 3 | 13 |
| α-helix | 1139-1150 | 12 | |
| β-strand | 1158-1160 | 3 | 13 |
| α-helix | 1163-1166 | 4 | |
| β-strand | 1177-1181 | 5 | 13 |
| α-helix | 1188-1198 | 11 | |
| β-strand | 1207-1211 | 5 | 13 |
| β-strand | 1214 | 1 | 14 |
| α-helix | 1217-1244 | 28 | |
| α-helix | 1248-1268 | 21 | |
| α-helix | 1280-1286 | 7 | |
| α-helix | 1293-1306 | 14 | |
| α-helix | 1337-1348 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone H3.2 | A, E | protein | 136 | Xenopus laevis | P84233 (AlphaFold model) |
| Histone H4 | B, F | protein | 103 | Xenopus laevis | P62799 (AlphaFold model) |
| Histone H2A | C, G | protein | 130 | Xenopus laevis | P06897 (AlphaFold model) |
| Histone H2B 1.1 | D, H | protein | 125 | Xenopus laevis | P02281 (AlphaFold model) |
| DNA (167-mer) | I | DNA | 167 | synthetic construct | |
| DNA (167-mer) | J | DNA | 167 | synthetic construct | |
| Transcription regulatory protein SNF2 | O | protein | 735 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P22082 |
>5X0X_1 Histone H3.2 (chains A, E) MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTE LLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTI MPKDIQLARRIRGERA
>5X0X_2 Histone H4 (chains B, F) MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
>5X0X_3 Histone H2A (chains C, G) MSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT AEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKK TESSKSAKSK
>5X0X_4 Histone H2B 1.1 (chains D, H) PEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMS IMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTK YTSAK
>5X0X_5 DNA (167-MER) (chains I) ATCGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAA ACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCA GGCACGTGTCAGATATATACATCCGATAGCTTGTCGAGAAGTACGAT
>5X0X_6 DNA (167-MER) (chains J) ATCGTACTTCTCGACAAGCTATCGGATGTATATATCTGACACGTGCCTGGAGACTAGGGA GTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTA GAGCTGTCTACGACCAATTGAGCGGCCTCGGCACCGGGATTCTCGAT
>5X0X_7 Transcription regulatory protein SNF2 (chains O) AYIKLLDQTKDTRITHLLRQTNAFLDSLTRAVKDQQKYTKEMIDSHIKEASEEVDDLSMV PKMKDEEYDDDDDNSNVDYYNVAHRIKEDIKKQPSILVGGTLKDYQIKGLQWMVSLFNNH LNGILADEMGLGKTIQTISLLTYLYEMKNIRGPYLVIVPLSTLSNWSSEFAKWAPTLRTI SFKGSPNERKAKQAKIRAGEFDVVLTTFEYIIKERALLSKVKWVHMIIDEGHRMKNAQSK LSLTLNTHYHADYRLILTGTPLQNNLPELWALLNFVLPKIFNSVKSFDEWFNTPFANTGG QDKIELSEEETLLVIRRLHKVLRPFLLRRLKKDVEKELPDKVEKVVKCKMSALQQIMYQQ MLKYRRLFIGDQNNKKMVGLRGFNNQIMQLKKICNHPFVFEEVEDQINPTRETNDDIWRV AGKFELLDRILPKLKATGHRVLIFFQMTQIMDIMEDFLRYINIKYLRLDGHTKSDERSEL LRLFNAPDSEYLCFILSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQKNE VRILRLITTNSVEEVILERAYKKLDIDGKVIQAGKFDNKSTSEEQEALLRSLLDAEEERR KKRESGVEEEEELKDSEINEILARNDEEMAVLTRMDEDRSKKEEELGVKSRLLEKSELPD IYSRDIGAELKREESESAAVYNGRGARERKTATYNDNMSEEQWLRQFEVSDDEKNDKQAR KQRTKKEDKSEAIDG
Mechanism of chromatin remodelling revealed by the Snf2-nucleosome structure. Liu, X., Li, M., Xia, X. et al. Nature (2017) 544:440-445. DOI 10.1038/nature22036 · PubMed
Other PDB entries of the same protein (UniProt P84233 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 5X0X directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.