6nzo

Set2 bound to nucleosome

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

Histone H3

Xenopus laevis

UniProt A0A310TTQ1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 9 DNA 2 Histone H4 × 2 (P62799) Ubiquitin-60S ribosomal protein L40,Histone H2A × 2 (P0CH09,Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 1 DNA (149-MER) × 1 Histone-lysine N-methyltransferase × 1 (G0S676) ZINC ION × 3 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A310TTQ1_XENLA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136

Histone H4

Xenopus laevis

UniProt P62799

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 9 DNA 2 Histone H3 × 2 (A0A310TTQ1) Ubiquitin-60S ribosomal protein L40,Histone H2A × 2 (P0CH09,Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 1 DNA (149-MER) × 1 Histone-lysine N-methyltransferase × 1 (G0S676) ZINC ION × 3 Consistent with all polymers

Other States of the Same Protein in the Database

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

Ubiquitin-60S ribosomal protein L40,Histone H2A

Xenopus laevis

UniProt P0CH09

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 9 DNA 2 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 1 DNA (149-MER) × 1 Histone-lysine N-methyltransferase × 1 (G0S676) ZINC ION × 3 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name RL40B_YEAST
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 21–95; UniProt 1–75 Author chain G; PDBConstruct 21–95; UniProt 1–75

Ubiquitin-60S ribosomal protein L40,Histone H2A

Xenopus laevis

UniProt Q6AZJ8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 9 DNA 2 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 1 DNA (149-MER) × 1 Histone-lysine N-methyltransferase × 1 (G0S676) ZINC ION × 3 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q6AZJ8_XENLA
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 109–221; UniProt 18–130 Author chain G; PDBConstruct 109–221; UniProt 18–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 9 DNA 2 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Ubiquitin-60S ribosomal protein L40,Histone H2A × 2 (P0CH09,Q6AZJ8) DNA (149-MER) × 1 DNA (149-MER) × 1 Histone-lysine N-methyltransferase × 1 (G0S676) ZINC ION × 3 Consistent with all polymers

Other States of the Same Protein in the Database

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

Histone-lysine N-methyltransferase

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

UniProt G0S676

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information Heteromer Protein 9 DNA 2 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Ubiquitin-60S ribosomal protein L40,Histone H2A × 2 (P0CH09,Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (149-MER) × 1 DNA (149-MER) × 1 ZINC ION × 3 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name G0S676_CHATD
Isoform —
PDB entities 7
Chains and sequence ranges Author chain S; PDBConstruct 1–939; UniProt 1–939

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_id6nzo
Deposition date deposition_date2019-02-14
Structure title titleSet2 bound to nucleosome
Keywords keywordsSet2, nucleosome, chromatin, KMT, GENE REGULATION; GENE REGULATION
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.

6nzo__assembly_1__model_1

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

Download this curve (.dat)

6nzo__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.

6nzo__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)43.02 Å
Rg (electron density)41.11 Å
Total Rg41.61 Å
Atom count13738
Residues1275
Excluded volume225330 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6nzo__assembly_1__model_1 undecameric (11) 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 (8)

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6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6nzoA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id6nzoH00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
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7. Citations (1)