9e00

Cryo-EM structure of human DNMT3A2-DNMT3B3 complex bound to di-nucleosome

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone H3.2

Homo sapiens

UniProt Q71DI3

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 24 DNA 2 Histone H4 × 4 (P62805) Histone H2A × 4 Histone H2B × 4 DNA (321-MER) × 1 DNA (321-MER) × 1 Isoform 3 of DNA (cytosine-5)-methyltransferase 3B × 4 (Q9UBC3) DNA (cytosine-5)-methyltransferase 3A × 4 (Q9Y6K1) ZINC ION × 9 S-ADENOSYL-L-HOMOCYSTEINE × 4 Consistent with all polymers

Other States of the Same Protein in the Database

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 Author chain M; PDBConstruct 1–135; UniProt 2–136 Author chain Q; PDBConstruct 1–135; UniProt 2–136

Histone H4

Homo sapiens

UniProt P62805

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 24 DNA 2 Histone H3.2 × 4 (Q71DI3) Histone H2A × 4 Histone H2B × 4 DNA (321-MER) × 1 DNA (321-MER) × 1 Isoform 3 of DNA (cytosine-5)-methyltransferase 3B × 4 (Q9UBC3) DNA (cytosine-5)-methyltransferase 3A × 4 (Q9Y6K1) ZINC ION × 9 S-ADENOSYL-L-HOMOCYSTEINE × 4 Consistent with all polymers

Other States of the Same Protein in the Database

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 Author chain N; PDBConstruct 1–103; UniProt 1–103 Author chain R; PDBConstruct 1–103; UniProt 1–103

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

Homo sapiens

UniProt Q9UBC3

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 24 DNA 2 Histone H3.2 × 4 (Q71DI3) Histone H4 × 4 (P62805) Histone H2A × 4 Histone H2B × 4 DNA (321-MER) × 1 DNA (321-MER) × 1 DNA (cytosine-5)-methyltransferase 3A × 4 (Q9Y6K1) ZINC ION × 9 S-ADENOSYL-L-HOMOCYSTEINE × 4 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DNM3B_HUMAN
Isoform Q9UBC3-3
PDB entities 7
Chains and sequence ranges Author chain L; PDBConstruct 1–773; UniProt 1–770 Author chain V; PDBConstruct 1–773; UniProt 1–770 Author chain X; 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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 24 DNA 2 Histone H3.2 × 4 (Q71DI3) Histone H4 × 4 (P62805) Histone H2A × 4 Histone H2B × 4 DNA (321-MER) × 1 DNA (321-MER) × 1 Isoform 3 of DNA (cytosine-5)-methyltransferase 3B × 4 (Q9UBC3) ZINC ION × 9 S-ADENOSYL-L-HOMOCYSTEINE × 4 Consistent with all polymers

Other States of the Same Protein in the Database

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 U; PDBConstruct 1–689; UniProt 224–912 Author chain W; 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e00
Deposition date deposition_date2024-10-17
Structure title titleCryo-EM structure of human DNMT3A2-DNMT3B3 complex bound to di-nucleosome
Keywords keywordsDNMT3A2, DNMT3B3, DNA methylation, di-nucleosome, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

9e00__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

9e00__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9e00__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)70.59 Å
Rg (electron density)70.35 Å
Total Rg70.33 Å
Atom count43873
Residues4462
Excluded volume739470 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9e00__assembly_1__model_1 26-meric (26) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (10)

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7. Citations (1)