8x31

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

Method: ELECTRON MICROSCOPY Dmax: 151.4 Å Quality: GOOD

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

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain L; UniProt 1–113 Not recorded Chromatin modification-related protein × 1 (A0A8H4C0Q6) Histone acetyltransferase × 1 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 1 (Q540A3,A0A8H8UL58) 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 6.20 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 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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain L; UniProt 1–392 Not recorded Chromatin modification-related protein × 1 (A0A8H4C0Q6) Histone acetyltransferase × 1 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 1 (Q540A3,A0A8H8UL58) 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 6.20 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 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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain N; UniProt 1–120 Not recorded Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) Histone acetyltransferase × 1 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 1 (Q540A3,A0A8H8UL58) 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 6.20 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 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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain K; UniProt 1–445 Not recorded Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) Chromatin modification-related protein × 1 (A0A8H4C0Q6) glutathione transferase,Enhancer of polycomb-like protein × 1 (Q540A3,A0A8H8UL58) 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 6.20 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 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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain M; UniProt 50–400 Not recorded Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.20 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 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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain M; UniProt 1–218 Not recorded Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.20 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 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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) Chromatin modification-related protein × 1 (A0A8H4C0Q6) Histone acetyltransferase × 1 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 1 (Q540A3,A0A8H8UL58) 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 6.20 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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain B; UniProt 1–102 Chain F; UniProt 1–102 Not recorded Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) Chromatin modification-related protein × 1 (A0A8H4C0Q6) Histone acetyltransferase × 1 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 1 (Q540A3,A0A8H8UL58) 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 6.20 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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain C; UniProt 1–134 Chain G; UniProt 1–134 Not recorded Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) Chromatin modification-related protein × 1 (A0A8H4C0Q6) Histone acetyltransferase × 1 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 1 (Q540A3,A0A8H8UL58) 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 6.20 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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain D; UniProt 1–131 Chain H; UniProt 1–131 Not recorded Maltose/maltodextrin-binding periplasmic protein,Chromatin modification-related protein EAF6 × 1 (P0AEX9,A0A6A5PYU5) Chromatin modification-related protein × 1 (A0A8H4C0Q6) Histone acetyltransferase × 1 (A0A6A5Q414) glutathione transferase,Enhancer of polycomb-like protein × 1 (Q540A3,A0A8H8UL58) 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 6.20 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 8x31

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8x31
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8x31
Deposition date deposition_date2023-11-10
Structure title titleThe piccolo NuA4 bound to the H2A.Z nucleosome complex with Ac-CoA at resetting state
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_guinier46.59
Radius of gyration Rg (electron density) rg_electron45.61
Forward intensity I(0) i01345700000.00
Molecular weight molecular_weight245830.0 kDa
Excluded volume excluded_volume283610 ų
Envelope volume envelope_volume444520 ų
Hydration-shell volume shell_volume80676 ų
Envelope diameter envelope_diameter153.4
Shell Rg shell_rg50.85
Envelope Rg envelope_rg44.58
Shape Rg shape_rg45.57
Total Rg total_rg45.91
Total atoms total_atoms16944
Residues n_residues1642
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 dmax151.4
Rg (real space) rg_real46.42
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real1.3460e+09
I(0) uncertainty (real space) i0_real_error2.6460e+07
Rg (reciprocal space) rg_reciprocal46.59
I(0) (reciprocal space) i0_reciprocal1346000000.0000
Solution quality estimate total_estimate0.8833
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.4
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha132100000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.823

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)