9can

S.c INO80 in complex with Xenopus 0/40 nucleosome

Method: ELECTRON MICROSCOPY Dmax: 221.3 Å Quality: GOOD

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

Histone H3

Xenopus laevis

UniProt A0A310TTQ1

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: 20-meric(20) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (227-MER) × 1 DNA (227-MER) × 1 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) 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 3.30 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.

126 other PDB entries and 130 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A310TTQ1_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136

Histone H4

Xenopus laevis

UniProt A0A8J1LTD2

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: 20-meric(20) Consistent with all polymer counts Chain B; UniProt 14–116 Chain F; UniProt 14–116 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (227-MER) × 1 DNA (227-MER) × 1 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) 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 3.30 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.

33 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J1LTD2_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 14–116 Author chain F; PDBConstruct 1–103; UniProt 14–116

Histone H2A

Xenopus laevis

UniProt Q6AZJ8

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: 20-meric(20) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2B 1.1 × 2 (P02281) DNA (227-MER) × 1 DNA (227-MER) × 1 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) 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 3.30 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.

226 other PDB entries and 238 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6AZJ8_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–130; UniProt 1–130 Author chain G; PDBConstruct 1–130; UniProt 1–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

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: 20-meric(20) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) DNA (227-MER) × 1 DNA (227-MER) × 1 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) 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 3.30 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.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–123; UniProt 5–126 Author chain H; PDBConstruct 2–123; UniProt 5–126

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–DNA Heteromer Protein × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain Q; UniProt 1–1489 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (227-MER) × 1 DNA (227-MER) × 1 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 3.30 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 7
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–DNA Heteromer Protein × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain R; UniProt 1–755 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (227-MER) × 1 DNA (227-MER) × 1 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 3.30 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 8
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–DNA Heteromer Protein × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain S; UniProt 1–166 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (227-MER) × 1 DNA (227-MER) × 1 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 3.30 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 9
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–DNA Heteromer Protein × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain T; UniProt 1–463 Chain V; UniProt 1–463 Chain X; UniProt 1–463 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (227-MER) × 1 DNA (227-MER) × 1 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 3.30 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 10
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–DNA Heteromer Protein × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain U; UniProt 1–460 Chain W; UniProt 1–460 Chain Y; UniProt 1–460 Fragment:residues 1-460 Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (227-MER) × 1 DNA (227-MER) × 1 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 3.30 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 11
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–DNA Heteromer Protein × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain Z; UniProt 1–320 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) DNA (227-MER) × 1 DNA (227-MER) × 1 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 3.30 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 12
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 9can

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9can
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9can
Deposition date deposition_date2024-06-17
Structure title titleS.c INO80 in complex with Xenopus 0/40 nucleosome
Keywords keywordsChromatin Remodeler, nucleosome, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier64.22
Radius of gyration Rg (electron density) rg_electron62.86
Forward intensity I(0) i06120270000.00
Molecular weight molecular_weight605080.0 kDa
Excluded volume excluded_volume735060 ų
Envelope volume envelope_volume1149600 ų
Hydration-shell volume shell_volume148240 ų
Envelope diameter envelope_diameter216.4
Shell Rg shell_rg67.84
Envelope Rg envelope_rg61.12
Shape Rg shape_rg62.80
Total Rg total_rg63.14
Total atoms total_atoms42187
Residues n_residues4937
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 dmax221.3
Rg (real space) rg_real64.10
Rg uncertainty (real space) rg_real_error2.24
I(0) (real space) i0_real6.1200e+09
I(0) uncertainty (real space) i0_real_error1.3540e+08
Rg (reciprocal space) rg_reciprocal64.30
I(0) (reciprocal space) i0_reciprocal6122000000.0000
Solution quality estimate total_estimate0.8760
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary73.8
Skewness Skewness skewness0.244
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0006
Highest regularization parameter α highest_alpha457700000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.846; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.854

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)