8x30

Structure of piccolo NuA4 and H2A.Z nucleosome 2:1 complex

Method: ELECTRON MICROSCOPY Dmax: 193.6 Å Quality: GOOD

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

Histone acetyltransferase

Saccharomyces cerevisiae

UniProt A0A6A5Q414

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: heptadecameric(17) Consistent with all polymer counts Chain K; UniProt 1–445 Chain O; UniProt 1–445 Not recorded glutathione transferase,Enhancer of polycomb-like protein × 2 (Q540A3,A0A8H8UL58) Chromatin modification-related protein × 2 (A0A8H4C0Q6) Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) DNA (146-MER) × 2 Histone H3 × 2 (A0A6A5Q536) Histone H4 × 2 (A0A6A5Q1V3) Histone H2A × 2 (A0A6A5Q818) Histone H2B × 2 (A0A6A5PZQ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q414_YEASX
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 25–469; UniProt 1–445 Author chain O; PDBConstruct 25–469; UniProt 1–445

glutathione transferase,Enhancer of polycomb-like protein

Saccharomyces cerevisiae

UniProt A0A8H8UL58

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: heptadecameric(17) Consistent with all polymer counts Chain M; UniProt 50–400 Chain Q; UniProt 50–400 Not recorded Histone acetyltransferase × 2 (A0A6A5Q414) Chromatin modification-related protein × 2 (A0A8H4C0Q6) Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) DNA (146-MER) × 2 Histone H3 × 2 (A0A6A5Q536) Histone H4 × 2 (A0A6A5Q1V3) Histone H2A × 2 (A0A6A5Q818) Histone H2B × 2 (A0A6A5PZQ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8H8UL58_YEASX
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 236–586; UniProt 50–400 Author chain Q; PDBConstruct 236–586; UniProt 50–400

glutathione transferase,Enhancer of polycomb-like protein

Saccharomyces cerevisiae

UniProt Q540A3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: heptadecameric(17) Consistent with all polymer counts Chain M; UniProt 1–218 Chain Q; UniProt 1–218 Not recorded Histone acetyltransferase × 2 (A0A6A5Q414) Chromatin modification-related protein × 2 (A0A8H4C0Q6) Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) DNA (146-MER) × 2 Histone H3 × 2 (A0A6A5Q536) Histone H4 × 2 (A0A6A5Q1V3) Histone H2A × 2 (A0A6A5Q818) Histone H2B × 2 (A0A6A5PZQ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q540A3_SCHJA
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 1–218; UniProt 1–218 Author chain Q; PDBConstruct 1–218; UniProt 1–218

Chromatin modification-related protein

Saccharomyces cerevisiae

UniProt A0A8H4C0Q6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: heptadecameric(17) Consistent with all polymer counts Chain N; UniProt 1–120 Chain R; UniProt 1–120 Not recorded Histone acetyltransferase × 2 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 2 (Q540A3,A0A8H8UL58) Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) DNA (146-MER) × 2 Histone H3 × 2 (A0A6A5Q536) Histone H4 × 2 (A0A6A5Q1V3) Histone H2A × 2 (A0A6A5Q818) Histone H2B × 2 (A0A6A5PZQ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8H4C0Q6_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain N; PDBConstruct 1–120; UniProt 1–120 Author chain R; PDBConstruct 1–120; UniProt 1–120

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

Saccharomyces cerevisiae

UniProt A0A6A5PYU5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: heptadecameric(17) Consistent with all polymer counts Chain P; UniProt 1–113 Not recorded Histone acetyltransferase × 2 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 2 (Q540A3,A0A8H8UL58) Chromatin modification-related protein × 2 (A0A8H4C0Q6) DNA (146-MER) × 2 Histone H3 × 2 (A0A6A5Q536) Histone H4 × 2 (A0A6A5Q1V3) Histone H2A × 2 (A0A6A5Q818) Histone H2B × 2 (A0A6A5PZQ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PYU5_YEASX
Isoform
PDB entities 4
Chains and sequence ranges Author chain P; 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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: heptadecameric(17) Consistent with all polymer counts Chain P; UniProt 1–392 Not recorded Histone acetyltransferase × 2 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 2 (Q540A3,A0A8H8UL58) Chromatin modification-related protein × 2 (A0A8H4C0Q6) DNA (146-MER) × 2 Histone H3 × 2 (A0A6A5Q536) Histone H4 × 2 (A0A6A5Q1V3) Histone H2A × 2 (A0A6A5Q818) Histone H2B × 2 (A0A6A5PZQ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain P; PDBConstruct 1–392; UniProt 1–392

Histone H3

Saccharomyces cerevisiae

UniProt A0A6A5Q536

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: heptadecameric(17) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded Histone acetyltransferase × 2 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 2 (Q540A3,A0A8H8UL58) Chromatin modification-related protein × 2 (A0A8H4C0Q6) Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) DNA (146-MER) × 2 Histone H4 × 2 (A0A6A5Q1V3) Histone H2A × 2 (A0A6A5Q818) Histone H2B × 2 (A0A6A5PZQ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: heptadecameric(17) Consistent with all polymer counts Chain B; UniProt 1–102 Chain F; UniProt 1–102 Not recorded Histone acetyltransferase × 2 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 2 (Q540A3,A0A8H8UL58) Chromatin modification-related protein × 2 (A0A8H4C0Q6) Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) DNA (146-MER) × 2 Histone H3 × 2 (A0A6A5Q536) Histone H2A × 2 (A0A6A5Q818) Histone H2B × 2 (A0A6A5PZQ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: heptadecameric(17) Consistent with all polymer counts Chain C; UniProt 1–134 Chain G; UniProt 1–134 Not recorded Histone acetyltransferase × 2 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 2 (Q540A3,A0A8H8UL58) Chromatin modification-related protein × 2 (A0A8H4C0Q6) Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) DNA (146-MER) × 2 Histone H3 × 2 (A0A6A5Q536) Histone H4 × 2 (A0A6A5Q1V3) Histone H2B × 2 (A0A6A5PZQ7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 DNA 2 PDB declaration: heptadecameric(17) Consistent with all polymer counts Chain D; UniProt 1–131 Chain H; UniProt 1–131 Not recorded Histone acetyltransferase × 2 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 2 (Q540A3,A0A8H8UL58) Chromatin modification-related protein × 2 (A0A8H4C0Q6) Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) DNA (146-MER) × 2 Histone H3 × 2 (A0A6A5Q536) Histone H4 × 2 (A0A6A5Q1V3) Histone H2A × 2 (A0A6A5Q818) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8x30

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8x30
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8x30
Deposition date deposition_date2023-11-10
Structure title titleStructure of piccolo NuA4 and H2A.Z nucleosome 2:1 complex
Keywords keywordsNua4, nucleosome, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier52.62
Radius of gyration Rg (electron density) rg_electron53.82
Forward intensity I(0) i01956560000.00
Molecular weight molecular_weight311580.0 kDa
Excluded volume excluded_volume366490 ų
Envelope volume envelope_volume583700 ų
Hydration-shell volume shell_volume95124 ų
Envelope diameter envelope_diameter212.4
Shell Rg shell_rg53.50
Envelope Rg envelope_rg52.81
Shape Rg shape_rg53.89
Total Rg total_rg53.61
Total atoms total_atoms21579
Residues n_residues2196
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax193.6
Rg (real space) rg_real52.75
Rg uncertainty (real space) rg_real_error2.12
I(0) (real space) i0_real1.9570e+09
I(0) uncertainty (real space) i0_real_error4.2090e+07
Rg (reciprocal space) rg_reciprocal52.52
I(0) (reciprocal space) i0_reciprocal1956000000.0000
Solution quality estimate total_estimate0.8273
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.5
Skewness Skewness skewness0.540
Kurtosis Kurtosis kurtosis0.317
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha216800000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.633; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.852

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)