9D3K: Two Dsup molecules

Two Dsup molecules in complex with the nucleosome open from both sides. Determined by electron microscopy at 2.7 Å resolution. Released 13 Aug 2025.

Method: Electron microscopy
Resolution: 2.7 Å
Organisms: Homo sapiens, synthetic construct, Ramazzottius varieornatus
Chains: 12
Atoms: 9,678
Mol. weight: 142.46 kDa
Released: 13 Aug 2025

Explore 9D3K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9D3K contains 35 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: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	45-55	11
α-helix	64-75	12
β-strand	83-84	2	1
α-helix	86-113	28
β-strand	118-119	2	2
α-helix	121-130	10

Chain B: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	26-28	3
α-helix	31-40	10
β-strand	45-46	2	2
α-helix	50-75	26
β-strand	80-81	2	1
α-helix	82	1
α-helix	83-92	10
β-strand	96-98	3	3

Chain C: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	17-21	5
α-helix	27-36	10
β-strand	42-43	2	4
α-helix	46-72	27
β-strand	77-78	2	5
α-helix	80-88	9
α-helix	91-96	6
β-strand	100-102	3	6

Chain D: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	38-48	11
β-strand	53-54	2	5
α-helix	56-83	28
β-strand	88-89	2	4
α-helix	91-101	11
α-helix	104-122	19

Chain E: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	45-56	12
α-helix	64-75	12
β-strand	83-84	2	7
α-helix	86-113	28
β-strand	118-119	2	8
α-helix	121-130	10

Chain F: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	25-28	4
α-helix	31-40	10
β-strand	45-46	2	8
α-helix	50-75	26
β-strand	80-81	2	7
α-helix	83-91	9
β-strand	96-98	3	6

Chain G: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	18-21	4
α-helix	27-36	10
β-strand	42-43	2	9
α-helix	47-72	26
β-strand	77-78	2	10
α-helix	80-88	9
α-helix	91-96	6
β-strand	100-102	3	3

Chain H: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	38-48	11
β-strand	53-54	2	10
α-helix	56-83	28
β-strand	88-89	2	9
α-helix	91-101	11
α-helix	104-121	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone H3.2	A, E	protein	95	Homo sapiens	Q71DI3 (AlphaFold model)
Histone H4	B, F	protein	79	Homo sapiens	P62805 (AlphaFold model)
Histone H2A type 2-A	C, G	protein	102	Homo sapiens	Q6FI13 (AlphaFold model)
Histone H2B type 1-M	D	protein	90	Homo sapiens	Q99879 (AlphaFold model)
Histone H2B type 1-M	H	protein	90	Homo sapiens	Q99879 (AlphaFold model)
601 DNA	J	DNA	94	synthetic construct
601 DNA	I	DNA	94	synthetic construct
Damage suppressor protein	K, L	protein	8	Ramazzottius varieornatus

Sequence of entity 1 (A, E), FASTA

>9D3K_1 Histone H3.2 (chains A, E)
YRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYL
VGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

Sequence of entity 2 (B, F), FASTA

>9D3K_2 Histone H4 (chains B, F)
RDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVT
AMDVVYALKRQGRTLYGFG

Sequence of entity 3 (C, G), FASTA

>9D3K_3 Histone H2A type 2-A (chains C, G)
KSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNK
KTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLL

Sequence of entity 4 (D), FASTA

>9D3K_4 Histone H2B type 1-M (chains D)
KESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSRE
IQTAVRLLLPGELAKHAVSEGTKAVTKYTS

Sequence of entity 5 (H), FASTA

>9D3K_5 Histone H2B type 1-M (chains H)
ESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREI
QTAVRLLLPGELAKHAVSEGTKAVTKYTSS

Sequence of entity 6 (J), FASTA

>9D3K_6 601 DNA (chains J)
TGGAGACTAGGGAGTAATCCCCTTGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGT
TTAAGCGGTGCTAGAGCTGTCTACGACCAATTGA

Sequence of entity 7 (I), FASTA

>9D3K_7 601 DNA (chains I)
TCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGT
TTTAACCGCCAAGGGGATTACTCCCTAGTCTCCA

Sequence of entity 8 (K, L), FASTA

>9D3K_8 Damage suppressor protein (chains K, L)
PPRRSSRL

Primary citation

Structural basis of nucleosome recognition by the conserved Dsup and HMGN nucleosome-binding motif. Alegrio-Louro, J., Cruz-Becerra, G., Kassavetis, G.A. et al. Genes Dev (2025) 39:1155-1161. DOI 10.1101/gad.352720.125 · PubMed

Other PDB entries of the same protein (UniProt Q71DI3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2X4W 1.5 Å, Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1.
4MZG 1.7 Å, Crystal structure of human Spindlin1 bound to histone H3K4me3 peptide
2X4Y 1.7 Å, Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1.
2X4X 1.85 Å, Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1.
4OUC 1.9 Å, Structure of human haspin in complex with histone H3 substrate
5VAC 1.95 Å, Crystal Structure of ATXR5 SET domain in complex with K36me3 histone H3 peptide
6ACE 1.98 Å, histone lysine desuccinylase Sirt5 in complex with succinyl peptide H3K122
7UVA 1.98 Å, Crystal structure of KDM2A histone demethylase catalytic domain in complex with an H3C36…
5B0Z 1.99 Å, The crystal structure of the nucleosome containing H3.2, at 1.98 A resolution
3R93 2.06 Å, Crystal structure of the chromo domain of M-phase phosphoprotein 8 bound to H3K9Me3…
4MZF 2.1 Å, Crystal structure of human Spindlin1 bound to histone H3(K4me3-R8me2a) peptide
4MZH 2.2 Å, Crystal structure of human Spindlin1 bound to histone H3(K4me3-R8me2s) peptide

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