9e3u

Cryo-EM structure of DNMT 3A2/3B3 tetramer bound to a di-nucleosome with a 25 base-pair linker

Method: ELECTRON MICROSCOPY Dmax: 200.6 Å Quality: GOOD

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

Histone H3.2

Homo sapiens

UniProt Q71DI3

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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded Histone H4 × 2 (P62805) Histone H2A × 2 Histone H2B × 2 (A0A1B8Y854) Isoform 3 of DNA (cytosine-5)-methyltransferase 3B × 3 (Q9UBC3) DNA (165-MER) × 1 DNA (165-MER) × 1 DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) ZN ZINC ION × 9 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.90 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.

139 other PDB entries and 157 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_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 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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H2A × 2 Histone H2B × 2 (A0A1B8Y854) Isoform 3 of DNA (cytosine-5)-methyltransferase 3B × 3 (Q9UBC3) DNA (165-MER) × 1 DNA (165-MER) × 1 DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) ZN ZINC ION × 9 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.90 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 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Histone H2B

Homo sapiens

UniProt A0A1B8Y854

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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A × 2 Isoform 3 of DNA (cytosine-5)-methyltransferase 3B × 3 (Q9UBC3) DNA (165-MER) × 1 DNA (165-MER) × 1 DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) ZN ZINC ION × 9 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.90 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A1B8Y854_XENTR
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 3 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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain L; UniProt 1–770 Chain V; UniProt 1–770 Chain Z; UniProt 1–770 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A × 2 Histone H2B × 2 (A0A1B8Y854) DNA (165-MER) × 1 DNA (165-MER) × 1 DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) ZN ZINC ION × 9 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.90 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 Q9UBC3-3
PDB entities 5
Chains and sequence ranges Author chain L; PDBConstruct 1–773; UniProt 1–770 Author chain V; PDBConstruct 1–773; UniProt 1–770 Author chain Z; PDBConstruct 1–773; UniProt 1–770

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 × 13 DNA 2 PDB declaration: 15-meric(15) Consistent with all polymer counts Chain U; UniProt 224–912 Chain Y; UniProt 224–912 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A × 2 Histone H2B × 2 (A0A1B8Y854) Isoform 3 of DNA (cytosine-5)-methyltransferase 3B × 3 (Q9UBC3) DNA (165-MER) × 1 DNA (165-MER) × 1 ZN ZINC ION × 9 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.90 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 U; PDBConstruct 1–689; UniProt 224–912 Author chain Y; 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 9e3u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e3u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e3u
Deposition date deposition_date2024-10-24
Structure title titleCryo-EM structure of DNMT 3A2/3B3 tetramer bound to a di-nucleosome with a 25 base-pair linker
Keywords keywordsDNA methylation, DNMT 3A2/3B3, di-nucleosome, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.70
Radius of gyration Rg (electron density) rg_electron57.75
Forward intensity I(0) i02476490000.00
Molecular weight molecular_weight344820.0 kDa
Excluded volume excluded_volume401390 ų
Envelope volume envelope_volume707330 ų
Hydration-shell volume shell_volume102630 ų
Envelope diameter envelope_diameter194.8
Shell Rg shell_rg60.73
Envelope Rg envelope_rg55.42
Shape Rg shape_rg57.75
Total Rg total_rg57.82
Total atoms total_atoms23771
Residues n_residues2447
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 dmax200.6
Rg (real space) rg_real57.71
Rg uncertainty (real space) rg_real_error2.28
I(0) (real space) i0_real2.4760e+09
I(0) uncertainty (real space) i0_real_error4.8960e+07
Rg (reciprocal space) rg_reciprocal57.67
I(0) (reciprocal space) i0_reciprocal2476000000.0000
Solution quality estimate total_estimate0.8732
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.9
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.417
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha165900000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.823

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)