8ets

Class1 of the INO80-Hexasome complex

Method: ELECTRON MICROSCOPY Dmax: 174.4 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 948–1432 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 3.04 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 1–485; UniProt 948–1432

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 12–755 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 3.04 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 1–744; UniProt 12–755

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 28–166 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 3.04 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 1–139; UniProt 28–166

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 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 3.04 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 15–471 Chain W; UniProt 15–471 Chain Y; UniProt 15–471 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 3.04 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 1–457; UniProt 15–471 Author chain W; PDBConstruct 1–457; UniProt 15–471 Author chain Y; PDBConstruct 1–457; UniProt 15–471

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 3.04 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 8ets

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ets
Deposition date deposition_date2022-10-17
Structure title titleClass1 of the INO80-Hexasome complex
Keywords keywordsChromatin Remodeler, hexasome, 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_guinier52.52
Radius of gyration Rg (electron density) rg_electron52.27
Forward intensity I(0) i02359210000.00
Molecular weight molecular_weight408040.0 kDa
Excluded volume excluded_volume512510 ų
Envelope volume envelope_volume727620 ų
Hydration-shell volume shell_volume114650 ų
Envelope diameter envelope_diameter189.0
Shell Rg shell_rg56.95
Envelope Rg envelope_rg52.06
Shape Rg shape_rg52.32
Total Rg total_rg52.24
Total atoms total_atoms28670
Residues n_residues3656
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 dmax174.4
Rg (real space) rg_real52.55
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real2.3590e+09
I(0) uncertainty (real space) i0_real_error4.4100e+07
Rg (reciprocal space) rg_reciprocal52.50
I(0) (reciprocal space) i0_reciprocal2359000000.0000
Solution quality estimate total_estimate0.8505
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.0
Skewness Skewness skewness0.439
Kurtosis Kurtosis kurtosis-0.058
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha354300000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.638

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)