7xyg

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

Method: ELECTRON MICROSCOPY Dmax: 148.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone H2A

Drosophila melanogaster

UniProt P84051

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain C; UniProt 2–124 Chain G; UniProt 2–124 Not recorded 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain D; UniProt 1–123 Chain H; UniProt 1–123 Not recorded 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

21 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain K; UniProt 1–922 Not recorded Histone H2A × 2 (P84051) Histone H2B × 2 (P02283) DNA (167-MER) × 1 DNA (167-MER) × 1 Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

23 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

18 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

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.

SAXS scattering curve SAXS Profile

SAXS profile for 7xyg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7xyg
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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

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier45.26
Radius of gyration Rg (electron density) rg_electron44.34
Forward intensity I(0) i01404590000.00
Molecular weight molecular_weight250950.0 kDa
Excluded volume excluded_volume289700 ų
Envelope volume envelope_volume423990 ų
Hydration-shell volume shell_volume79722 ų
Envelope diameter envelope_diameter151.9
Shell Rg shell_rg49.35
Envelope Rg envelope_rg43.06
Shape Rg shape_rg44.27
Total Rg total_rg44.67
Total atoms total_atoms17273
Residues n_residues1704
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax148.4
Rg (real space) rg_real45.12
Rg uncertainty (real space) rg_real_error1.19
I(0) (real space) i0_real1.4050e+09
I(0) uncertainty (real space) i0_real_error2.2600e+07
Rg (reciprocal space) rg_reciprocal45.26
I(0) (reciprocal space) i0_reciprocal1405000000.0000
Solution quality estimate total_estimate0.8188
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.1
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.418
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha136400000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)