8x31

The piccolo NuA4 bound to the H2A.Z nucleosome complex with Ac-CoA at resetting state

Method: ELECTRON MICROSCOPY

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6

Saccharomyces cerevisiae

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 12 DNA 2	Chromatin modification-related protein × 1 （A0A8H4C0Q6） Histone acetyltransferase × 1 （A0A6A5Q414） glutathione transferase,Enhancer of polycomb-like protein × 1 （A0A8H8UL58,Q540A3） DNA (146-MER) × 2 Histone H3 × 2 （A0A6A5Q536） Histone H4 × 2 （A0A6A5Q1V3） Histone H2A × 2 （A0A6A5Q818） Histone H2B × 2 （A0A6A5PZQ7）	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A6A5PYU5_YEASX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain L； PDBConstruct 425–537； UniProt 1–113

Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6

Saccharomyces cerevisiae

UniProt P0AEX9

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 12 DNA 2	Chromatin modification-related protein × 1 （A0A8H4C0Q6） Histone acetyltransferase × 1 （A0A6A5Q414） glutathione transferase,Enhancer of polycomb-like protein × 1 （A0A8H8UL58,Q540A3） DNA (146-MER) × 2 Histone H3 × 2 （A0A6A5Q536） Histone H4 × 2 （A0A6A5Q1V3） Histone H2A × 2 （A0A6A5Q818） Histone H2B × 2 （A0A6A5PZQ7）	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MALE_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain L； PDBConstruct 1–392； UniProt 1–392

Chromatin modification-related protein

Saccharomyces cerevisiae

UniProt A0A8H4C0Q6

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 12 DNA 2	Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 （A0A6A5PYU5,P0AEX9） Histone acetyltransferase × 1 （A0A6A5Q414） glutathione transferase,Enhancer of polycomb-like protein × 1 （A0A8H8UL58,Q540A3） DNA (146-MER) × 2 Histone H3 × 2 （A0A6A5Q536） Histone H4 × 2 （A0A6A5Q1V3） Histone H2A × 2 （A0A6A5Q818） Histone H2B × 2 （A0A6A5PZQ7）	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A8H4C0Q6_YEASX
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain N； PDBConstruct 1–120； UniProt 1–120

Histone acetyltransferase

Saccharomyces cerevisiae

UniProt A0A6A5Q414

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 12 DNA 2	Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 （A0A6A5PYU5,P0AEX9） Chromatin modification-related protein × 1 （A0A8H4C0Q6） glutathione transferase,Enhancer of polycomb-like protein × 1 （A0A8H8UL58,Q540A3） DNA (146-MER) × 2 Histone H3 × 2 （A0A6A5Q536） Histone H4 × 2 （A0A6A5Q1V3） Histone H2A × 2 （A0A6A5Q818） Histone H2B × 2 （A0A6A5PZQ7）	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A6A5Q414_YEASX
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain K； PDBConstruct 25–469； UniProt 1–445

glutathione transferase,Enhancer of polycomb-like protein

Saccharomyces cerevisiae

UniProt A0A8H8UL58

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 12 DNA 2	Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 （A0A6A5PYU5,P0AEX9） Chromatin modification-related protein × 1 （A0A8H4C0Q6） Histone acetyltransferase × 1 （A0A6A5Q414） DNA (146-MER) × 2 Histone H3 × 2 （A0A6A5Q536） Histone H4 × 2 （A0A6A5Q1V3） Histone H2A × 2 （A0A6A5Q818） Histone H2B × 2 （A0A6A5PZQ7）	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A8H8UL58_YEASX
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain M； PDBConstruct 236–586； UniProt 50–400

glutathione transferase,Enhancer of polycomb-like protein

Saccharomyces cerevisiae

UniProt Q540A3

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 12 DNA 2	Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 （A0A6A5PYU5,P0AEX9） Chromatin modification-related protein × 1 （A0A8H4C0Q6） Histone acetyltransferase × 1 （A0A6A5Q414） DNA (146-MER) × 2 Histone H3 × 2 （A0A6A5Q536） Histone H4 × 2 （A0A6A5Q1V3） Histone H2A × 2 （A0A6A5Q818） Histone H2B × 2 （A0A6A5PZQ7）	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q540A3_SCHJA
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain M； PDBConstruct 1–218； UniProt 1–218

Histone H3

Saccharomyces cerevisiae

UniProt A0A6A5Q536

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 12 DNA 2	Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 （A0A6A5PYU5,P0AEX9） Chromatin modification-related protein × 1 （A0A8H4C0Q6） Histone acetyltransferase × 1 （A0A6A5Q414） glutathione transferase,Enhancer of polycomb-like protein × 1 （A0A8H8UL58,Q540A3） DNA (146-MER) × 2 Histone H4 × 2 （A0A6A5Q1V3） Histone H2A × 2 （A0A6A5Q818） Histone H2B × 2 （A0A6A5PZQ7）	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A6A5Q536_YEASX
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain A； PDBConstruct 1–136； UniProt 1–136 Author chain E； PDBConstruct 1–136； UniProt 1–136

Histone H4

Saccharomyces cerevisiae

UniProt A0A6A5Q1V3

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 12 DNA 2	Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 （A0A6A5PYU5,P0AEX9） Chromatin modification-related protein × 1 （A0A8H4C0Q6） Histone acetyltransferase × 1 （A0A6A5Q414） glutathione transferase,Enhancer of polycomb-like protein × 1 （A0A8H8UL58,Q540A3） DNA (146-MER) × 2 Histone H3 × 2 （A0A6A5Q536） Histone H2A × 2 （A0A6A5Q818） Histone H2B × 2 （A0A6A5PZQ7）	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A6A5Q1V3_YEASX
Isoform	—
PDB entities	7
Chains and sequence ranges	Author chain B； PDBConstruct 1–102； UniProt 1–102 Author chain F； PDBConstruct 1–102； UniProt 1–102

Histone H2A

Saccharomyces cerevisiae

UniProt A0A6A5Q818

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 12 DNA 2	Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 （A0A6A5PYU5,P0AEX9） Chromatin modification-related protein × 1 （A0A8H4C0Q6） Histone acetyltransferase × 1 （A0A6A5Q414） glutathione transferase,Enhancer of polycomb-like protein × 1 （A0A8H8UL58,Q540A3） DNA (146-MER) × 2 Histone H3 × 2 （A0A6A5Q536） Histone H4 × 2 （A0A6A5Q1V3） Histone H2B × 2 （A0A6A5PZQ7）	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A6A5Q818_YEASX
Isoform	—
PDB entities	8
Chains and sequence ranges	Author chain C； PDBConstruct 1–134； UniProt 1–134 Author chain G； PDBConstruct 1–134； UniProt 1–134

Histone H2B

Saccharomyces cerevisiae

UniProt A0A6A5PZQ7

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 12 DNA 2	Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 （A0A6A5PYU5,P0AEX9） Chromatin modification-related protein × 1 （A0A8H4C0Q6） Histone acetyltransferase × 1 （A0A6A5Q414） glutathione transferase,Enhancer of polycomb-like protein × 1 （A0A8H8UL58,Q540A3） DNA (146-MER) × 2 Histone H3 × 2 （A0A6A5Q536） Histone H4 × 2 （A0A6A5Q1V3） Histone H2A × 2 （A0A6A5Q818）	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A6A5PZQ7_YEASX
Isoform	—
PDB entities	9
Chains and sequence ranges	Author chain D； PDBConstruct 1–131； UniProt 1–131 Author chain H； PDBConstruct 1–131； UniProt 1–131

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8x31
Deposition date deposition_date	2023-11-10
Structure title title	The piccolo NuA4 bound to the H2A.Z nucleosome complex with Ac-CoA at resetting state
Keywords keywords	Nua4, nucleosome, GENE REGULATION; GENE REGULATION
Experimental Method method	ELECTRON MICROSCOPY

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8x31__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8x31__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

8x31__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	46.59 Å
Rg (electron density)	45.61 Å
Total Rg	45.91 Å
Atom count	16944
Residues	1642
Excluded volume	283610 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`8x31__assembly_1__model_1`	tetradecameric （14）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (9)

Entity 1 Entity 1 polymer

Description description	Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6
Molecular weight formula_weight	59471.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L
Atom count atom_count	16944

MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELVKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNSSSNNNNNNNNNNLGIEGRISEFENLYFQGHMTDELKSYEALKAELKKSLQDRREQEDTFDNLQQEIYDKETEYFSHNSNNNHSGHGGAHGSKSHYSGNIIKGFDTFSKSHHSHADSAFNNNDRIFSLSSATYVKQQHGQSQND

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	;Escherichia coli 'BL21-Gold(DE3)pLysS AG' ;

Entity 2 Entity 2 polymer

Description description	Chromatin modification-related protein
Molecular weight formula_weight	13828.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	N

MDPSLVLEQTIQDVSNLPSEFRYLLEEIGSNDLKLIEEKKKYEQKESQIHKFIRQQGSIPKHPQEDGLDKEIKESLLKCQSLQREKCVLANTALFLIARHLNKLEKNIALLEEDGVLAPV

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	;Escherichia coli 'BL21-Gold(DE3)pLysS AG' ;

Entity 3 Entity 3 polymer

Description description	Histone acetyltransferase
Molecular weight formula_weight	55419.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K

MGSSHHHHHHSQDHENLYFQGAGSMSHDGKEEPGIAKKINSVDDIIIKCQCWVQKNDEERLAEILSINTRKAPPKFYVHYVNYNKRLDEWITTDRINLDKEVLYPKLKATDEDNKKQKKKKATNTSETPQDSLQDGVDGFSRENTDVMDLDNLNVQGIKDENISHEDEIKKLRTSGSMTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDEDFIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDDYVSFFEIDGRKQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQRMGYGKLLIEFSYELSKKENKVGSPEKPLSDLGLLSYRAYWSDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLNILRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKPPVFTASQLRFAW

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	;Escherichia coli 'BL21-Gold(DE3)pLysS AG' ;

Entity 4 Entity 4 polymer

Description description	glutathione transferase,Enhancer of polycomb-like protein
Molecular weight formula_weight	69286.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M

MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPKSDLVPRGSENLYFQGHMSSNSRFRHRKISVKQHLKIYLPNDLKHLDKDELQQREVVEIETGVEKNEEKEVHLHRILQMGSGHTKHKDYIPTPDASMTWNEYDKFYTGSFQETTSYIKFSATVEDCCGTNYNMDERDETFLNEQVNKGSSDILTEDEFEILCSSFEHAIHERQPFLSMDPESILSFEELKPTLIKSDMADFNLRNQLNHEINSHKTHFITQFDPVSQMNTRPLIQLIEKFGSKIYDYWRERKIEVNGYEIFPQLKFERPGEKEEIDPYVCFRRREVRHPRKTRRIDILNSQRLRALHQELKNAKDLALLVAKRENVSLNWINDELKIFDQRVKIKNLKRSLNISGEDDDLINHKRKRPT

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	;Escherichia coli 'BL21-Gold(DE3)pLysS AG' ;

Entity 5 Entity 5 polymer

Description description	DNA (146-MER)
Molecular weight formula_weight	45054.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polydeoxyribonucleotide
Chain IDs strand_id	I,J

ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT

Source Source

Source organism organism	Saccharomyces cerevisiae
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	;Escherichia coli 'BL21-Gold(DE3)pLysS AG' ;

Entity 6 Entity 6 polymer

Description description	Histone H3
Molecular weight formula_weight	15391.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,E

MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAKRVTIQKKDIKLARRLRGERS

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	;Escherichia coli 'BL21-Gold(DE3)pLysS AG' ;

Entity 7 Entity 7 polymer

Description description	Histone H4
Molecular weight formula_weight	11338.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,F

MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFG

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	;Escherichia coli 'BL21-Gold(DE3)pLysS AG' ;

Entity 8 Entity 8 polymer

Description description	Histone H2A
Molecular weight formula_weight	14313.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,G

MSGKAHGGKGKSGAKDSGSLRSQSSSARAGLQFPVGRIKRYLKRHATGRTRVGSKAAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDDELDSLIRATIASGGVLPHINKALLLKVEKKGSKK

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	;Escherichia coli 'BL21-Gold(DE3)pLysS AG' ;

Entity 9 Entity 9 polymer

Description description	Histone H2B
Molecular weight formula_weight	14280.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,H

MSAKAEKKPASKAPAEKKPAAKKTSTSTDGKKRSKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	4932
Host organism host_organism	;Escherichia coli 'BL21-Gold(DE3)pLysS AG' ;

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Resolution resolution	6.20 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	15537

The piccolo NuA4 bound to the H2A.Z nucleosome complex with Ac-CoA at resetting state

1. Protein Identity and Related Structures Protein Identity & Related Structures

Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Chromatin modification-related protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Histone acetyltransferase

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

glutathione transferase,Enhancer of polycomb-like protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

glutathione transferase,Enhancer of polycomb-like protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Histone H3

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Histone H4

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Histone H2A

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Histone H2B

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer