8eu9

Class1 of the INO80-Nucleosome complex

Method: ELECTRON MICROSCOPY Dmax: 175.9 Å Quality: GOOD

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

Chromatin-remodeling ATPase INO80

OrganismNot specified

UniProt P53115

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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain Q; UniProt 948–1440 Not recorded Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 3.48 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.

16 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INO80_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain Q; PDBConstruct 1–493; UniProt 948–1440

Actin-related protein 5

OrganismNot specified

UniProt P53946

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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain R; UniProt 1–755 Not recorded Chromatin-remodeling ATPase INO80 × 1 (P53115) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 3.48 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP5_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain R; PDBConstruct 1–755; UniProt 1–755

Chromatin-remodeling complex subunit IES6

OrganismNot specified

UniProt P32617

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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain S; UniProt 28–162 Not recorded Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 3.48 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IES6_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain S; PDBConstruct 1–135; UniProt 28–162

RuvB-like protein 1

OrganismNot specified

UniProt Q03940

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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain T; UniProt 21–463 Chain V; UniProt 21–463 Chain X; UniProt 21–463 Not recorded Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 3.48 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUVB1_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain T; PDBConstruct 1–443; UniProt 21–463 Author chain V; PDBConstruct 1–443; UniProt 21–463 Author chain X; PDBConstruct 1–443; UniProt 21–463

RuvB-like protein 2

OrganismNot specified

UniProt Q12464

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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain U; UniProt 15–460 Chain W; UniProt 15–460 Chain Y; UniProt 15–460 Not recorded Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) Ino eighty subunit 2 × 1 (P40154) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 3.48 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.

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

View Construct and Data Evidence
UniProt name RUVB2_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain U; PDBConstruct 1–446; UniProt 15–460 Author chain W; PDBConstruct 1–446; UniProt 15–460 Author chain Y; PDBConstruct 1–446; UniProt 15–460

Ino eighty subunit 2

OrganismNot specified

UniProt P40154

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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain Z; UniProt 293–320 Not recorded Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 3.48 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IES2_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain Z; PDBConstruct 1–28; UniProt 293–320

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8eu9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8eu9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8eu9
Deposition date deposition_date2022-10-18
Structure title titleClass1 of the INO80-Nucleosome complex
Keywords keywordsChromatin Remodeler, hexasome, DNA BINDING PROTEIN, DNA BINDING PROTEIN-Hydrolase complex; DNA BINDING PROTEIN/Hydrolase
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.89
Radius of gyration Rg (electron density) rg_electron51.58
Forward intensity I(0) i02348850000.00
Molecular weight molecular_weight405830.0 kDa
Excluded volume excluded_volume509140 ų
Envelope volume envelope_volume707810 ų
Hydration-shell volume shell_volume112680 ų
Envelope diameter envelope_diameter186.6
Shell Rg shell_rg56.52
Envelope Rg envelope_rg51.54
Shape Rg shape_rg51.62
Total Rg total_rg51.59
Total atoms total_atoms28517
Residues n_residues3660
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 dmax175.9
Rg (real space) rg_real51.90
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real2.3490e+09
I(0) uncertainty (real space) i0_real_error4.3080e+07
Rg (reciprocal space) rg_reciprocal51.87
I(0) (reciprocal space) i0_reciprocal2349000000.0000
Solution quality estimate total_estimate0.8506
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.5
Skewness Skewness skewness0.429
Kurtosis Kurtosis kurtosis-0.066
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha329900000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.782; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.725

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)