7xyg

Cryo-EM structure of Fft3-nucleosome complex with Fft3 bound to SHL+3 position of the nucleosome

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

Histone H2A

Drosophila melanogaster

UniProt P84051

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 H2B × 2 (P02283) DNA (167-MER) × 1 DNA (167-MER) × 1 ATP-dependent helicase fft3 × 1 (O42861) Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2A_DROME
Isoform —
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–123; UniProt 2–124 Author chain G; PDBConstruct 1–123; UniProt 2–124

Histone H2B

Drosophila melanogaster

UniProt P02283

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 H2A × 2 (P84051) DNA (167-MER) × 1 DNA (167-MER) × 1 ATP-dependent helicase fft3 × 1 (O42861) Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2B_DROME
Isoform —
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–123; UniProt 1–123 Author chain H; PDBConstruct 1–123; UniProt 1–123

ATP-dependent helicase fft3

Schizosaccharomyces pombe 972h-

UniProt O42861

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 H2A × 2 (P84051) Histone H2B × 2 (P02283) DNA (167-MER) × 1 DNA (167-MER) × 1 Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FFT3_SCHPO
Isoform —
PDB entities 5
Chains and sequence ranges Author chain K; PDBConstruct 1–922; UniProt 1–922

Histone H3

Drosophila melanogaster

UniProt P02299

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 H2A × 2 (P84051) Histone H2B × 2 (P02283) DNA (167-MER) × 1 DNA (167-MER) × 1 ATP-dependent helicase fft3 × 1 (O42861) Histone H4 × 2 (P84040) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H3_DROME
Isoform —
PDB entities 6
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

Histone H4

Drosophila melanogaster

UniProt P84040

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 H2A × 2 (P84051) Histone H2B × 2 (P02283) DNA (167-MER) × 1 DNA (167-MER) × 1 ATP-dependent helicase fft3 × 1 (O42861) Histone H3 × 2 (P02299) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H4_DROME
Isoform —
PDB entities 7
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

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_id7xyg
Deposition date deposition_date2022-06-01
Structure title titleCryo-EM structure of Fft3-nucleosome complex with Fft3 bound to SHL+3 position of the nucleosome
Keywords keywordsDNA binding, remodeler, nucleosome, Fft3-nucleosome complex, 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.

7xyg__assembly_1__model_1

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

Download this curve (.dat)

7xyg__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.

7xyg__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)45.26 Å
Rg (electron density)44.34 Å
Total Rg44.67 Å
Atom count17273
Residues1704
Excluded volume289700 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 7xyg__assembly_1__model_1 11-meric (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 (7)

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7. Citations (1)