9q7u

Composite map for Cryo-EM structure of DNMT3A2-DNMT3B3 tetramer bound to 167H3K36me2-nucleosome

Method: ELECTRON MICROSCOPY Dmax: 178.1 Å Quality: GOOD

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

Histone H3

Xenopus laevis

UniProt A0A310TTQ1

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (162-MER) × 1 DNA (162-MER) × 1 Isoform 7 of DNA (cytosine-5)-methyltransferase 3B × 2 (Q9UBC3) DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) ZN ZINC ION × 9 SAO 5'-S-[(3S)-3-azaniumyl-3-carboxypropyl]-5'-thioadenosine × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

126 other PDB entries and 130 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A310TTQ1_XENLA
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

Xenopus laevis

UniProt P62799

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (162-MER) × 1 DNA (162-MER) × 1 Isoform 7 of DNA (cytosine-5)-methyltransferase 3B × 2 (Q9UBC3) DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) ZN ZINC ION × 9 SAO 5'-S-[(3S)-3-azaniumyl-3-carboxypropyl]-5'-thioadenosine × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

354 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Histone H2A type 1

Xenopus laevis

UniProt P06897

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (162-MER) × 1 DNA (162-MER) × 1 Isoform 7 of DNA (cytosine-5)-methyltransferase 3B × 2 (Q9UBC3) DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) ZN ZINC ION × 9 SAO 5'-S-[(3S)-3-azaniumyl-3-carboxypropyl]-5'-thioadenosine × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

136 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_XENLA
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 1.1

Xenopus laevis

UniProt P02281

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) DNA (162-MER) × 1 DNA (162-MER) × 1 Isoform 7 of DNA (cytosine-5)-methyltransferase 3B × 2 (Q9UBC3) DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) ZN ZINC ION × 9 SAO 5'-S-[(3S)-3-azaniumyl-3-carboxypropyl]-5'-thioadenosine × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–123; UniProt 5–126 Author chain H; PDBConstruct 2–123; UniProt 5–126

Isoform 7 of DNA (cytosine-5)-methyltransferase 3B

Homo sapiens

UniProt Q9UBC3

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain V; UniProt 118–694 Chain Z; UniProt 118–694 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (162-MER) × 1 DNA (162-MER) × 1 DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) ZN ZINC ION × 9 SAO 5'-S-[(3S)-3-azaniumyl-3-carboxypropyl]-5'-thioadenosine × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

45 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNM3B_HUMAN
Isoform Q9UBC3-7
PDB entities 7
Chains and sequence ranges Author chain V; PDBConstruct 1–580; UniProt 118–694 Author chain Z; PDBConstruct 1–580; UniProt 118–694

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain K; UniProt 224–912 Chain L; UniProt 224–912 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (162-MER) × 1 DNA (162-MER) × 1 Isoform 7 of DNA (cytosine-5)-methyltransferase 3B × 2 (Q9UBC3) ZN ZINC ION × 9 SAO 5'-S-[(3S)-3-azaniumyl-3-carboxypropyl]-5'-thioadenosine × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 8
Chains and sequence ranges Author chain K; PDBConstruct 1–689; UniProt 224–912 Author chain L; PDBConstruct 1–689; UniProt 224–912

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 9q7u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9q7u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9q7u
Deposition date deposition_date2025-08-25
Structure title titleComposite map for Cryo-EM structure of DNMT3A2-DNMT3B3 tetramer bound to 167H3K36me2-nucleosome
Keywords keywordsDNMT3A2-DNMT3B3, DNA methylation, 167H3K36me2-nucleosome, 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_guinier55.43
Radius of gyration Rg (electron density) rg_electron55.28
Forward intensity I(0) i02738790000.00
Molecular weight molecular_weight370270.0 kDa
Excluded volume excluded_volume434590 ų
Envelope volume envelope_volume718120 ų
Hydration-shell volume shell_volume105930 ų
Envelope diameter envelope_diameter183.1
Shell Rg shell_rg61.31
Envelope Rg envelope_rg53.08
Shape Rg shape_rg55.28
Total Rg total_rg55.40
Total atoms total_atoms48116
Residues n_residues2682
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 dmax178.1
Rg (real space) rg_real55.25
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real2.7390e+09
I(0) uncertainty (real space) i0_real_error6.2540e+07
Rg (reciprocal space) rg_reciprocal55.56
I(0) (reciprocal space) i0_reciprocal2740000000.0000
Solution quality estimate total_estimate0.8855
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.0
Skewness Skewness skewness0.155
Kurtosis Kurtosis kurtosis-0.565
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha244000000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.724

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)