6JXD: Histone H3.1

Human nucleosome core particle with cohesive end DNA termini. Determined by X-ray diffraction at 2.25 Å resolution. Released 15 Jan 2020.

Method
X-ray diffraction
Resolution
2.25 Å
Organism
Homo sapiens
Chains
10
Atoms
12,227
Mol. weight
179.14 kDa
Ligands
MN
Released
15 Jan 2020

Explore 6JXD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6JXD contains 39 α-helices and 20 β-strands across 8 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-helix45-5612
α-helix64-7613
β-strand83-8421
α-helix86-11328
β-strand118-11922
α-helix121-13111
Chain B: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix25-284
α-helix31-4010
β-strand45-4622
α-helix50-7526
β-strand80-8121
α-helix83-9210
β-strand97-9823
Chain C: 6 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix17-215
α-helix27-359
β-strand42-4324
α-helix47-7226
β-strand77-7825
α-helix80-889
α-helix91-966
β-strand100-10236
α-helix113-1153
Chains D and H: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix35-4511
β-strand50-5125
α-helix53-8028
β-strand85-8624
α-helix88-9811
α-helix101-11919
Chain E: 5 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix41-422
α-helix45-5612
α-helix64-7815
β-strand83-8427
α-helix86-11328
β-strand118-11928
α-helix121-13010
Chain F: 5 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix20-223
α-helix25-284
α-helix31-4010
β-strand45-4628
α-helix50-7526
β-strand80-8127
α-helix83-9210
β-strand96-9836
Chain G: 6 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix17-204
α-helix27-3610
β-strand42-4329
α-helix47-7226
β-strand77-78210
α-helix80-8910
α-helix91-966
β-strand101-10223
α-helix113-1153

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone H3.1Aprotein98Homo sapiensP68431 (AlphaFold model)
Histone H4Bprotein82Homo sapiensP62805 (AlphaFold model)
Histone H2A type 1-B/ECprotein107Homo sapiensP04908 (AlphaFold model)
Histone H2B type 1-JD, Hprotein97Homo sapiensP06899 (AlphaFold model)
Histone H3.1Eprotein97Homo sapiensP68431 (AlphaFold model)
Histone H4Fprotein87Homo sapiensP62805 (AlphaFold model)
Histone H2A type 1-B/EGprotein106Homo sapiensP04908 (AlphaFold model)
DNA (147-mer)IDNA147Homo sapiens
DNA (147-mer)JDNA147Homo sapiens
Sequence of entity 1 (A), FASTA
>6JXD_1 Histone H3.1 (chains A)
PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACE
AYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Sequence of entity 2 (B), FASTA
>6JXD_2 Histone H4 (chains B)
VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKT
VTAMDVVYALKRQGRTLYGFGG
Sequence of entity 3 (C), FASTA
>6JXD_3 Histone H2A type 1-B/E (chains C)
RKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAAR
DNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPK
Sequence of entity 4 (D, H), FASTA
>6JXD_4 Histone H2B type 1-J (chains D, H)
RKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRST
ITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
Sequence of entity 5 (E), FASTA
>6JXD_5 Histone H3.1 (chains E)
PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACE
AYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGER
Sequence of entity 6 (F), FASTA
>6JXD_6 Histone H4 (chains F)
KRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEH
AKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 7 (G), FASTA
>6JXD_7 Histone H2A type 1-B/E (chains G)
KAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARD
NKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPK
Sequence of entity 8 (I), FASTA
>6JXD_8 DNA (147-MER) (chains I)
CATATATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAAC
GCACGTACGCGCTGTCTACCGCGTTTTAACCGCCACTAGAAGCGCTTACTAGTCTCCAGG
CACGTGTGAGACCGGCATATATGGTAC
Sequence of entity 9 (J), FASTA
>6JXD_9 DNA (147-MER) (chains J)
CATATATGCCGGTCTCACACGTGCCTGGAGACTAGTAAGCGCTTCTAGTGGCGGTTAAAA
CGCGGTAGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGTCTACGACCAATTGAG
CGGCCTCGGCACCGGGATATATGGTAC

Ligands and cofactors

IDNameFormulaCopies
MNManganese (II) ionMn17

Primary citation

PARP1 exhibits enhanced association and catalytic efficiency with gamma H2A.X-nucleosome. Sharma, D., De Falco, L., Padavattan, S. et al. Nat Commun (2019) 10:5751-5751. DOI 10.1038/s41467-019-13641-0 · PubMed

Other PDB entries of the same protein (UniProt P68431 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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