8qzm

Structure of DNMT3A1 UDR region bound to H2AK119ub nucleosome

Method: ELECTRON MICROSCOPY Dmax: 121.0 Å Quality: GOOD

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

Histone H3 (Fragment)

Homo sapiens

UniProt A0A7K7T3V7

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 (P62805) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 DNA (cytosine-5)-methyltransferase 3A × 1 (Q9Y6K1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;15 mM HEPES pH 7.5, 65 mM NaCl, 1 mM DTT, 0.1 mM S-Adenosyl methionine cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A7K7T3V7_9TYRA
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 H4

Homo sapiens

UniProt P62805

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 B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded Histone H3 (Fragment) × 2 (A0A7K7T3V7) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 DNA (cytosine-5)-methyltransferase 3A × 1 (Q9Y6K1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;15 mM HEPES pH 7.5, 65 mM NaCl, 1 mM DTT, 0.1 mM S-Adenosyl methionine cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103

Histone H2A type 1

Homo sapiens

UniProt P0C0S8

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 (Fragment) × 2 (A0A7K7T3V7) Histone H4 × 2 (P62805) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 DNA (cytosine-5)-methyltransferase 3A × 1 (Q9Y6K1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;15 mM HEPES pH 7.5, 65 mM NaCl, 1 mM DTT, 0.1 mM S-Adenosyl methionine cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

49 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_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-C/E/F/G/I

Homo sapiens

UniProt P62807

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 (Fragment) × 2 (A0A7K7T3V7) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) DNA (145-MER) × 1 DNA (145-MER) × 1 DNA (cytosine-5)-methyltransferase 3A × 1 (Q9Y6K1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;15 mM HEPES pH 7.5, 65 mM NaCl, 1 mM DTT, 0.1 mM S-Adenosyl methionine cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

79 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1C_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

DNA (cytosine-5)-methyltransferase 3A

Homo sapiens

UniProt Q9Y6K1

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 1–912 Not recorded Histone H3 (Fragment) × 2 (A0A7K7T3V7) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;15 mM HEPES pH 7.5, 65 mM NaCl, 1 mM DTT, 0.1 mM S-Adenosyl methionine cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

42 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNM3A_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 4–915; UniProt 1–912

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 8qzm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8qzm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8qzm
Deposition date deposition_date2023-10-27
Structure title titleStructure of DNMT3A1 UDR region bound to H2AK119ub nucleosome
Keywords keywordsChromatin, Nucleosome, methyltransferase, Ubiquitin, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.02
Radius of gyration Rg (electron density) rg_electron37.28
Forward intensity I(0) i0848119000.00
Molecular weight molecular_weight177870.0 kDa
Excluded volume excluded_volume197440 ų
Envelope volume envelope_volume293240 ų
Hydration-shell volume shell_volume63734 ų
Envelope diameter envelope_diameter119.4
Shell Rg shell_rg44.95
Envelope Rg envelope_rg36.71
Shape Rg shape_rg37.11
Total Rg total_rg38.00
Total atoms total_atoms12141
Residues n_residues1073
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 dmax121.0
Rg (real space) rg_real39.83
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real8.4810e+08
I(0) uncertainty (real space) i0_real_error1.4140e+07
Rg (reciprocal space) rg_reciprocal40.01
I(0) (reciprocal space) i0_reciprocal848300000.0000
Solution quality estimate total_estimate0.8359
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.5
Skewness Skewness skewness0.076
Kurtosis Kurtosis kurtosis-0.682
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha58580000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)