8euf

Class2 of the INO80-Nucleosome complex

Method: ELECTRON MICROSCOPY Dmax: 173.9 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 1–1489 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 3.41 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 1–1489; UniProt 1–1489

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 3.41 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 1–166 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 3.41 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 1–166; UniProt 1–166

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 1–463 Chain V; UniProt 1–463 Chain X; UniProt 1–463 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 3.41 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 1–463; UniProt 1–463 Author chain V; PDBConstruct 1–463; UniProt 1–463 Author chain X; PDBConstruct 1–463; UniProt 1–463

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 1–460 Chain W; UniProt 1–460 Chain Y; UniProt 1–460 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 3.41 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 1–460; UniProt 1–460 Author chain W; PDBConstruct 1–460; UniProt 1–460 Author chain Y; PDBConstruct 1–460; UniProt 1–460

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 1–320 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 3.41 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 1–320; 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.

SAXS scattering curve SAXS Profile

SAXS profile for 8euf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8euf
Deposition date deposition_date2022-10-18
Structure title titleClass2 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_electron51.66
Forward intensity I(0) i02367590000.00
Molecular weight molecular_weight408550.0 kDa
Excluded volume excluded_volume513040 ų
Envelope volume envelope_volume703020 ų
Hydration-shell volume shell_volume112350 ų
Envelope diameter envelope_diameter189.4
Shell Rg shell_rg56.37
Envelope Rg envelope_rg51.23
Shape Rg shape_rg51.71
Total Rg total_rg51.63
Total atoms total_atoms28707
Residues n_residues3664
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 dmax173.9
Rg (real space) rg_real51.90
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real2.3680e+09
I(0) uncertainty (real space) i0_real_error4.4450e+07
Rg (reciprocal space) rg_reciprocal51.87
I(0) (reciprocal space) i0_reciprocal2367000000.0000
Solution quality estimate total_estimate0.8515
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.8
Skewness Skewness skewness0.435
Kurtosis Kurtosis kurtosis-0.061
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha326400000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.802; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.679

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)