7zi4

Cryo-EM structure of the human INO80 complex bound to a WT nucleosome

Method: ELECTRON MICROSCOPY Dmax: 221.2 Å Quality: GOOD

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

RuvB-like 1

Homo sapiens

UniProt Q9Y265

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain A; UniProt 1–456 Chain C; UniProt 1–456 Chain E; UniProt 1–456 Not recorded RuvB-like 2 × 3 (Q9Y230) Chromatin-remodeling ATPase INO80 × 1 (Q9ULG1) Histone H4 × 2 (P62805) INO80 complex subunit B × 1 (Q9C086) Actin-related protein 5 × 1 (Q9H9F9) INO80 complex subunit C × 1 (Q6PI98) Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (158-MER) × 1 DNA (158-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4uL of sample applied to Quantifoil R2/2 Cu 300 mesh grids. blot parameters were wait time 30 sec, blot time 0.5 sec, blot force -8 Resolution 3.20 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.

35 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUVB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–456; UniProt 1–456 Author chain C; PDBConstruct 1–456; UniProt 1–456 Author chain E; PDBConstruct 1–456; UniProt 1–456

RuvB-like 2

Homo sapiens

UniProt Q9Y230

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain B; UniProt 1–463 Chain D; UniProt 1–463 Chain F; UniProt 1–463 Not recorded RuvB-like 1 × 3 (Q9Y265) Chromatin-remodeling ATPase INO80 × 1 (Q9ULG1) Histone H4 × 2 (P62805) INO80 complex subunit B × 1 (Q9C086) Actin-related protein 5 × 1 (Q9H9F9) INO80 complex subunit C × 1 (Q6PI98) Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (158-MER) × 1 DNA (158-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4uL of sample applied to Quantifoil R2/2 Cu 300 mesh grids. blot parameters were wait time 30 sec, blot time 0.5 sec, blot force -8 Resolution 3.20 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.

37 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUVB2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–463; UniProt 1–463 Author chain D; PDBConstruct 1–463; UniProt 1–463 Author chain F; PDBConstruct 1–463; UniProt 1–463

Chromatin-remodeling ATPase INO80

Homo sapiens

UniProt Q9ULG1

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain G; UniProt 1–1556 Not recorded RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Histone H4 × 2 (P62805) INO80 complex subunit B × 1 (Q9C086) Actin-related protein 5 × 1 (Q9H9F9) INO80 complex subunit C × 1 (Q6PI98) Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (158-MER) × 1 DNA (158-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4uL of sample applied to Quantifoil R2/2 Cu 300 mesh grids. blot parameters were wait time 30 sec, blot time 0.5 sec, blot force -8 Resolution 3.20 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INO80_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–1556; UniProt 1–1556

Histone H4

Homo sapiens

UniProt P62805

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain J; UniProt 1–103 Chain N; UniProt 1–103 Not recorded RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Chromatin-remodeling ATPase INO80 × 1 (Q9ULG1) INO80 complex subunit B × 1 (Q9C086) Actin-related protein 5 × 1 (Q9H9F9) INO80 complex subunit C × 1 (Q6PI98) Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (158-MER) × 1 DNA (158-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4uL of sample applied to Quantifoil R2/2 Cu 300 mesh grids. blot parameters were wait time 30 sec, blot time 0.5 sec, blot force -8 Resolution 3.20 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain J; PDBConstruct 1–103; UniProt 1–103 Author chain N; PDBConstruct 1–103; UniProt 1–103

INO80 complex subunit B

Homo sapiens

UniProt Q9C086

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain R; UniProt 1–356 Not recorded RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Chromatin-remodeling ATPase INO80 × 1 (Q9ULG1) Histone H4 × 2 (P62805) Actin-related protein 5 × 1 (Q9H9F9) INO80 complex subunit C × 1 (Q6PI98) Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (158-MER) × 1 DNA (158-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4uL of sample applied to Quantifoil R2/2 Cu 300 mesh grids. blot parameters were wait time 30 sec, blot time 0.5 sec, blot force -8 Resolution 3.20 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IN80B_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain R; PDBConstruct 1–356; UniProt 1–356

Actin-related protein 5

Homo sapiens

UniProt Q9H9F9

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain H; UniProt 1–607 Not recorded RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Chromatin-remodeling ATPase INO80 × 1 (Q9ULG1) Histone H4 × 2 (P62805) INO80 complex subunit B × 1 (Q9C086) INO80 complex subunit C × 1 (Q6PI98) Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (158-MER) × 1 DNA (158-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4uL of sample applied to Quantifoil R2/2 Cu 300 mesh grids. blot parameters were wait time 30 sec, blot time 0.5 sec, blot force -8 Resolution 3.20 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP5_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain H; PDBConstruct 1–607; UniProt 1–607

INO80 complex subunit C

Homo sapiens

UniProt Q6PI98

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain Q; UniProt 1–192 Not recorded RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Chromatin-remodeling ATPase INO80 × 1 (Q9ULG1) Histone H4 × 2 (P62805) INO80 complex subunit B × 1 (Q9C086) Actin-related protein 5 × 1 (Q9H9F9) Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (158-MER) × 1 DNA (158-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4uL of sample applied to Quantifoil R2/2 Cu 300 mesh grids. blot parameters were wait time 30 sec, blot time 0.5 sec, blot force -8 Resolution 3.20 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.

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

View Construct and Data Evidence
UniProt name IN80C_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain Q; PDBConstruct 1–192; UniProt 1–192

Histone H3.1

Homo sapiens

UniProt P68431

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain I; UniProt 1–136 Chain M; UniProt 1–136 Not recorded RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Chromatin-remodeling ATPase INO80 × 1 (Q9ULG1) Histone H4 × 2 (P62805) INO80 complex subunit B × 1 (Q9C086) Actin-related protein 5 × 1 (Q9H9F9) INO80 complex subunit C × 1 (Q6PI98) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (158-MER) × 1 DNA (158-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4uL of sample applied to Quantifoil R2/2 Cu 300 mesh grids. blot parameters were wait time 30 sec, blot time 0.5 sec, blot force -8 Resolution 3.20 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain I; PDBConstruct 1–136; UniProt 1–136 Author chain M; PDBConstruct 1–136; UniProt 1–136

Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain K; UniProt 1–130 Chain O; UniProt 1–130 Not recorded RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Chromatin-remodeling ATPase INO80 × 1 (Q9ULG1) Histone H4 × 2 (P62805) INO80 complex subunit B × 1 (Q9C086) Actin-related protein 5 × 1 (Q9H9F9) INO80 complex subunit C × 1 (Q6PI98) Histone H3.1 × 2 (P68431) Histone H2B type 1-J × 2 (P06899) DNA (158-MER) × 1 DNA (158-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4uL of sample applied to Quantifoil R2/2 Cu 300 mesh grids. blot parameters were wait time 30 sec, blot time 0.5 sec, blot force -8 Resolution 3.20 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain K; PDBConstruct 1–130; UniProt 1–130 Author chain O; PDBConstruct 1–130; UniProt 1–130

Histone H2B type 1-J

Homo sapiens

UniProt P06899

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain L; UniProt 1–126 Chain P; UniProt 1–126 Not recorded RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Chromatin-remodeling ATPase INO80 × 1 (Q9ULG1) Histone H4 × 2 (P62805) INO80 complex subunit B × 1 (Q9C086) Actin-related protein 5 × 1 (Q9H9F9) INO80 complex subunit C × 1 (Q6PI98) Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) DNA (158-MER) × 1 DNA (158-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;4uL of sample applied to Quantifoil R2/2 Cu 300 mesh grids. blot parameters were wait time 30 sec, blot time 0.5 sec, blot force -8 Resolution 3.20 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.

290 other PDB entries and 301 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1J_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain L; PDBConstruct 1–126; UniProt 1–126 Author chain P; PDBConstruct 1–126; UniProt 1–126

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 7zi4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7zi4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7zi4
Deposition date deposition_date2022-04-07
Structure title titleCryo-EM structure of the human INO80 complex bound to a WT nucleosome
Keywords keywordschromatin remodeler, transcription, replication, DNA repair, 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_guinier65.11
Radius of gyration Rg (electron density) rg_electron63.55
Forward intensity I(0) i06433040000.00
Molecular weight molecular_weight607600.0 kDa
Excluded volume excluded_volume731830 ų
Envelope volume envelope_volume1192700 ų
Hydration-shell volume shell_volume151780 ų
Envelope diameter envelope_diameter208.0
Shell Rg shell_rg69.35
Envelope Rg envelope_rg61.34
Shape Rg shape_rg63.49
Total Rg total_rg63.82
Total atoms total_atoms42294
Residues n_residues5000
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 dmax221.2
Rg (real space) rg_real64.86
Rg uncertainty (real space) rg_real_error2.00
I(0) (real space) i0_real6.4330e+09
I(0) uncertainty (real space) i0_real_error1.2610e+08
Rg (reciprocal space) rg_reciprocal65.28
I(0) (reciprocal space) i0_reciprocal6437000000.0000
Solution quality estimate total_estimate0.8144
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary73.7
Skewness Skewness skewness0.173
Kurtosis Kurtosis kurtosis-0.588
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha404800000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (1)

9. Files and Curves (10)