8haj

Cryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 2 (4.8 angstrom resolution)

Method: ELECTRON MICROSCOPY Dmax: 152.8 Å Quality: GOOD

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

Histone H3.1

Homo sapiens

UniProt P68431

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded Histone H4 × 2 Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (180-mer) × 2 Histone acetyltransferase p300 × 1 (Q09472) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.80 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 Histone H2B type 1-J × 2 (P06899) DNA (180-mer) × 2 Histone acetyltransferase p300 × 1 (Q09472) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.80 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

Histone H2B type 1-J

Homo sapiens

UniProt P06899

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 2–126 Chain H; UniProt 2–126 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 Histone H2A type 1-B/E × 2 (P04908) DNA (180-mer) × 2 Histone acetyltransferase p300 × 1 (Q09472) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.80 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.

290 other PDB entries and 301 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1J_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–125; UniProt 2–126 Author chain H; PDBConstruct 1–125; UniProt 2–126

Histone acetyltransferase p300

Homo sapiens

UniProt Q09472

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain K; UniProt 1048–1836 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (180-mer) × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.80 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.

58 other PDB entries and 92 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EP300_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain K; PDBConstruct 8–796; UniProt 1048–1836

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 8haj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8haj
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8haj
Deposition date deposition_date2022-10-26
Structure title titleCryo-EM structure of the p300 catalytic core bound to the H4K12acK16ac nucleosome, class 2 (4.8 angstrom resolution)
Keywords keywordsAcetyl taransferase, Complex, Nucleosome, TRANSFERASE, TRANSFERASE-DNA complex; TRANSFERASE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.35
Radius of gyration Rg (electron density) rg_electron46.31
Forward intensity I(0) i01466620000.00
Molecular weight molecular_weight250710.0 kDa
Excluded volume excluded_volume285850 ų
Envelope volume envelope_volume452340 ų
Hydration-shell volume shell_volume80124 ų
Envelope diameter envelope_diameter153.5
Shell Rg shell_rg51.98
Envelope Rg envelope_rg45.22
Shape Rg shape_rg46.26
Total Rg total_rg46.62
Total atoms total_atoms17214
Residues n_residues1629
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 dmax152.8
Rg (real space) rg_real47.22
Rg uncertainty (real space) rg_real_error1.88
I(0) (real space) i0_real1.4670e+09
I(0) uncertainty (real space) i0_real_error2.9710e+07
Rg (reciprocal space) rg_reciprocal47.35
I(0) (reciprocal space) i0_reciprocal1467000000.0000
Solution quality estimate total_estimate0.8826
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.5
Skewness Skewness skewness0.234
Kurtosis Kurtosis kurtosis-0.476
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha139100000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.730

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)