7ea5

Yeast Set2 bound to a nucleosome containing oncohistone mutations

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 Protein–DNA Heteromer Protein 9 DNA 2 Histone H4 × 2 Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) 601-DNA × 1 601-DNA × 1 Histone-lysine N-methyltransferase, H3 lysine-36 specific × 1 (A0A6V8RR65) ZINC ION × 3 S-ADENOSYLMETHIONINE × 1 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 1–101; UniProt 35–135 Author chain E; PDBConstruct 1–101; UniProt 35–135

Histone H2A

Xenopus laevis

UniProt Q6AZJ8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 Histone H2B × 2 (A0A1L8FQA5) 601-DNA × 1 601-DNA × 1 Histone-lysine N-methyltransferase, H3 lysine-36 specific × 1 (A0A6V8RR65) ZINC ION × 3 S-ADENOSYLMETHIONINE × 1 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 1–105; UniProt 14–118 Author chain G; PDBConstruct 1–105; UniProt 14–118

Histone H2B

Xenopus laevis

UniProt A0A1L8FQA5

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 Histone H2A × 2 (Q6AZJ8) 601-DNA × 1 601-DNA × 1 Histone-lysine N-methyltransferase, H3 lysine-36 specific × 1 (A0A6V8RR65) ZINC ION × 3 S-ADENOSYLMETHIONINE × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A1L8FQA5_XENLA
Isoform —
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–93; UniProt 32–124 Author chain H; PDBConstruct 1–93; UniProt 32–124

Histone-lysine N-methyltransferase, H3 lysine-36 specific

Saccharomyces cerevisiae

UniProt A0A6V8RR65

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A1L8FQA5) 601-DNA × 1 601-DNA × 1 ZINC ION × 3 S-ADENOSYLMETHIONINE × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A6V8RR65_YEASX
Isoform —
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–228; UniProt 33–260

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_id7ea5
Deposition date deposition_date2021-03-06
Structure title titleYeast Set2 bound to a nucleosome containing oncohistone mutations
Keywords keywordsmethyltransferase, Set2, nucleosome, H3K36M mutation, 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.

7ea5__assembly_1__model_1

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

Download this curve (.dat)

7ea5__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.

7ea5__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)44.60 Å
Rg (electron density)42.63 Å
Total Rg43.10 Å
Atom count13770
Residues1265
Excluded volume226130 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 7ea5__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 (9)

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6. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id7ea5A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7ea5B01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7ea5D01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7ea5E01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7ea5F01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7ea5H01
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)