9cb7

DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome

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

Histone H3

Saccharomyces cerevisiae

UniProt P61830

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 Histone H4 × 2 (P62799) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) DNA (227-MER) × 1 DNA (227-MER) × 1 Chromatin-remodeling ATPase INO80 × 1 (P53115) Ino eighty subunit 2 × 1 (P40154) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H3_YEAST
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 Protein–DNA Heteromer Protein 10 DNA 2 Histone H3 × 2 (P61830) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) DNA (227-MER) × 1 DNA (227-MER) × 1 Chromatin-remodeling ATPase INO80 × 1 (P53115) Ino eighty subunit 2 × 1 (P40154) 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

Histone H2A.1

Saccharomyces cerevisiae

UniProt P04911

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 Histone H3 × 2 (P61830) Histone H4 × 2 (P62799) Histone H2B.1 × 2 (P02293) DNA (227-MER) × 1 DNA (227-MER) × 1 Chromatin-remodeling ATPase INO80 × 1 (P53115) Ino eighty subunit 2 × 1 (P40154) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2A1_YEAST
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–132; UniProt 1–132 Author chain G; PDBConstruct 1–132; UniProt 1–132

Histone H2B.1

Saccharomyces cerevisiae

UniProt P02293

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 Histone H3 × 2 (P61830) Histone H4 × 2 (P62799) Histone H2A.1 × 2 (P04911) DNA (227-MER) × 1 DNA (227-MER) × 1 Chromatin-remodeling ATPase INO80 × 1 (P53115) Ino eighty subunit 2 × 1 (P40154) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2B1_YEAST
Isoform —
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–131; UniProt 1–131 Author chain H; PDBConstruct 1–131; UniProt 1–131

Chromatin-remodeling ATPase INO80

OrganismNot specified

UniProt P53115

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 Histone H3 × 2 (P61830) Histone H4 × 2 (P62799) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) DNA (227-MER) × 1 DNA (227-MER) × 1 Ino eighty subunit 2 × 1 (P40154) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name INO80_YEAST
Isoform —
PDB entities 7
Chains and sequence ranges Author chain Q; PDBConstruct 1–1489; UniProt 1–1489

Ino eighty subunit 2

OrganismNot specified

UniProt P40154

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 10 DNA 2 Histone H3 × 2 (P61830) Histone H4 × 2 (P62799) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) DNA (227-MER) × 1 DNA (227-MER) × 1 Chromatin-remodeling ATPase INO80 × 1 (P53115) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name IES2_YEAST
Isoform —
PDB entities 8
Chains and sequence ranges Author chain Z; PDBConstruct 1–320; UniProt 1–320

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_id9cb7
Deposition date deposition_date2024-06-18
Structure title titleDeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome
Keywords keywordsChromatin Remodeler, nucleosome, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
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.

9cb7__assembly_1__model_1

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

Download this curve (.dat)

9cb7__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.

9cb7__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)47.54 Å
Rg (electron density)46.73 Å
Total Rg46.98 Å
Atom count15448
Residues1493
Excluded volume255880 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9cb7__assembly_1__model_1 12-meric (12) 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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7. Citations (1)