8KCC: Probable histone H2A.7
Complex of DDM1-nucleosome(H2A.W) complex with DDM1 bound to SHL2. Determined by electron microscopy at 3.1 Å resolution. Released 26 Jun 2024.
- Method
- Electron microscopy
- Resolution
- 3.1 Å
- Organisms
- Arabidopsis thaliana, synthetic construct
- Chains
- 11
- Atoms
- 16,271
- Mol. weight
- 309.22 kDa
- Ligands
- BEF, ADP
- Released
- 26 Jun 2024
Explore 8KCC in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8KCC contains 64 α-helices and 40 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, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-30 | 5 | |
| α-helix | 36-46 | 11 | |
| β-strand | 51-52 | 2 | 1 |
| α-helix | 55-81 | 27 | |
| β-strand | 86-87 | 2 | 2 |
| α-helix | 89-98 | 10 | |
| α-helix | 100-105 | 6 | |
| β-strand | 109-110 | 2 | 3 |
Chain B: 5 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-29 | 4 | |
| α-helix | 36-46 | 11 | |
| β-strand | 51-52 | 2 | 4 |
| α-helix | 56-81 | 26 | |
| β-strand | 86-87 | 2 | 5 |
| α-helix | 89-98 | 10 | |
| α-helix | 100-105 | 6 | |
| β-strand | 110-111 | 2 | 6 |
Chains C and D: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 58-68 | 11 | |
| β-strand | 73-74 | 2 | 5 |
| α-helix | 76-103 | 28 | |
| β-strand | 108-109 | 2 | 4 |
| α-helix | 111-121 | 11 | |
| α-helix | 125-143 | 19 | |
Chains E and F: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 43-57 | 15 | |
| α-helix | 64-78 | 15 | |
| β-strand | 83-84 | 2 | 7 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 8 |
| α-helix | 121-131 | 11 | |
Chain G: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-28 | 3 | |
| α-helix | 31-41 | 11 | |
| β-strand | 45-46 | 2 | 8 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 7 |
| α-helix | 83-92 | 10 | |
| β-strand | 97-98 | 2 | 6 |
Chain H: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-24 | 4 | |
| α-helix | 31-41 | 11 | |
| β-strand | 45-46 | 2 | 10 |
| α-helix | 49-75 | 27 | |
| β-strand | 80-81 | 2 | 9 |
| α-helix | 83-92 | 10 | |
| β-strand | 96-97 | 2 | 3 |
Chain K: 30 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 184-193 | 10 | |
| α-helix | 204-219 | 16 | |
| β-strand | 223 | 1 | 11 |
| β-strand | 224-225 | 2 | 12 |
| β-strand | 226 | 1 | 13 |
| α-helix | 233-246 | 14 | |
| β-strand | 253-256 | 4 | 14 |
| α-helix | 259-271 | 13 | |
| β-strand | 278-281 | 4 | 14 |
| α-helix | 285-295 | 11 | |
| β-strand | 306-309 | 4 | 14 |
| α-helix | 311-317 | 7 | |
| α-helix | 318-322 | 5 | |
| β-strand | 327-333 | 7 | 14 |
| α-helix | 335-338 | 4 | |
| α-helix | 344-351 | 8 | |
| β-strand | 354-356 | 3 | 14 |
| β-strand | 358 | 1 | 11 |
| β-strand | 359-360 | 2 | 14 |
| β-strand | 361 | 1 | 13 |
| α-helix | 371-379 | 9 | |
| α-helix | 387-393 | 7 | |
| α-helix | 411-423 | 13 | |
| β-strand | 428-429 | 2 | 12 |
| α-helix | 441-442 | 2 | |
| β-strand | 443-451 | 9 | 15 |
| α-helix | 452-453 | 2 | |
| α-helix | 454-464 | 11 | |
| α-helix | 468-471 | 4 | |
| α-helix | 489-497 | 9 | |
| α-helix | 500-508 | 9 | |
| α-helix | 513-515 | 3 | |
| α-helix | 516-522 | 7 | |
| α-helix | 526-539 | 14 | |
| β-strand | 543-547 | 5 | 15 |
| α-helix | 550-563 | 14 | |
| β-strand | 567-570 | 4 | 15 |
| α-helix | 576-586 | 11 | |
| β-strand | 595-599 | 5 | 15 |
| β-strand | 614-617 | 4 | 15 |
| α-helix | 624-631 | 8 | |
| α-helix | 642 | 1 | |
| β-strand | 643-651 | 9 | 15 |
| α-helix | 655-670 | 16 | |
| α-helix | 706-710 | 5 | |
| α-helix | 712-714 | 3 | |
| α-helix | 715-722 | 8 | |
| β-strand | 744-745 | 2 | 15 |
| β-strand | 748-750 | 3 | 15 |
| α-helix | 760-763 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Probable histone H2A.7 | A, B | protein | 150 | Arabidopsis thaliana | Q9FJE8 (AlphaFold model) |
| Histone H2B.10 | C, D | protein | 145 | Arabidopsis thaliana | Q9FFC0 (AlphaFold model) |
| Histone H3.1 | E, F | protein | 136 | Arabidopsis thaliana | P59226 (AlphaFold model) |
| Histone H4 | G, H | protein | 103 | Arabidopsis thaliana | P59259 (AlphaFold model) |
| DNA (170-mer) | I | DNA | 170 | synthetic construct | |
| DNA (170-mer) | J | DNA | 170 | synthetic construct | |
| ATP-dependent DNA helicase DDM1 | K | protein | 764 | Arabidopsis thaliana | Q9XFH4 |
Sequence of entity 1 (A, B), FASTA
>8KCC_1 Probable histone H2A.7 (chains A, B)
MESTGKVKKAFGGRKPPGAPKTKSVSKSMKAGLQFPVGRITRFLKKGRYAQRLGGGAPVY
MAAVLEYLAAEVLELAGNAARDNKKSRIIPRHLLLAIRNDEELGKLLSGVTIAHGGVLPN
INSVLLPKKSATKPAEEKATKSPVKSPKKA
Sequence of entity 2 (C, D), FASTA
>8KCC_2 Histone H2B.10 (chains C, D)
MAKADKKPAEKKPAEKTPAAEPAAAAEKKPKAGKKLPKEPAGAGDKKKKRSKKNVETYKI
YIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAGESSKLARYNKKPTITSREIQTAVR
LVLPGELAKHAVSEGTKAVTKFTSS
Sequence of entity 3 (E, F), FASTA
>8KCC_3 Histone H3.1 (chains E, F)
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTE
LLIRKLPFQRLVREIAQDFKTDLRFQSSAVAALQEAAEAYLVGLFEDTNLCAIHAKRVTI
MPKDIQLARRIRGERA
Sequence of entity 4 (G, H), FASTA
>8KCC_4 Histone H4 (chains G, H)
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK
IFLENVIRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 5 (I), FASTA
>8KCC_5 DNA (170-MER) (chains I)
ATCCTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCT
TAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCT
CCAGGCACGTGTCACATATATACATCCTGTTCCAGTGCCGGTGTCGCGAT
Sequence of entity 6 (J), FASTA
>8KCC_6 DNA (170-MER) (chains J)
ATCGCGACACCGGCACTGGAACAGGATGTATATATGTGACACGTGCCTGGAGACTAGGGA
GTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTA
GAGCTGTCTACGACCAATTGAGCGGCCTCGGCACCGGGATTCTCCAGGAT
Sequence of entity 7 (K), FASTA
>8KCC_7 ATP-dependent DNA helicase DDM1 (chains K)
MVSLRSRKVIPASEMVSDGKTEKDASGDSPTSVLNEEENCEEKSVTVVEEEILLAKNGDS
SLISEAMAQEEEQLLKLREDEEKANNAGSAVAPNLNETQFTKLDELLTQTQLYSEFLLEK
MEDITINGIESESQKAEPEKTGRGRKRKAASQYNNTKAKRAVAAMISRSKEDGETINSDL
TEEETVIKLQNELCPLLTGGQLKSYQLKGVKWLISLWQNGLNGILADQMGLGKTIQTIGF
LSHLKGNGLDGPYLVIAPLSTLSNWFNEIARFTPSINAIIYHGDKNQRDELRRKHMPKTV
GPKFPIVITSYEVAMNDAKRILRHYPWKYVVIDEGHRLKNHKCKLLRELKHLKMDNKLLL
TGTPLQNNLSELWSLLNFILPDIFTSHDEFESWFDFSEKNKNEATKEEEEKRRAQVVSKL
HGILRPFILRRMKCDVELSLPRKKEIIMYATMTDHQKKFQEHLVNNTLEAHLGENAIRGQ
GWKGKLNNLVIQLRKNCNHPDLLQGQIDGSYLYPPVEEIVGQCGKFRLLERLLVRLFANN
HKVLIFSQWTKLLDIMDYYFSEKGFEVCRIDGSVKLDERRRQIKDFSDEKSSCSIFLLST
RAGGLGINLTAADTCILYDSDWNPQMDLQAMDRCHRIGQTKPVHVYRLSTAQSIETRVLK
RAYSKLKLEHVVIGQGQFHQERAKSSTPLEEEDILALLKEDETAEDKLIQTDISDADLDR
LLDRSDLTITAPGETQAAEAFPVKGPGWEVVLPSSGGMLSSLNS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| BEF | Beryllium trifluoride ion | Be F3 | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Primary citation
Mechanism of heterochromatin remodeling revealed by the DDM1 bound nucleosome structures. Zhang, H., Gu, Z., Zeng, Y. et al. Structure (2024) 32:1222-1230.e4. DOI 10.1016/j.str.2024.05.013 · PubMed
Other PDB entries of the same protein (UniProt Q9FJE8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9K41 2.81 Å, Cryo-EM structure of Arabidopsis thaliana H2A.W-nucleosome with Arabidopsis native 147bp…
- 9K46 2.85 Å, Cryo-EM structure of Arabidopsis thaliana H2A.W-H3.3-nucleosome with Arabidopsis native…
- 8J92 2.9 Å, Cryo-EM structure of nucleosome containing Arabidopsis thaliana H2A.W
- 7UX9 3.2 Å, Arabidopsis DDM1 bound to nucleosome (H2A.W, H2B, H3.3, H4, with 147 bp DNA)
- 8J90 4.71 Å, Cryo-EM structure of DDM1-nucleosome complex
Browse structure collections
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