6fhs

CryoEM Structure of INO80core

Method: ELECTRON MICROSCOPY Dmax: 173.9 Å Quality: GOOD

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

RuvB-like helicase

Chaetomium thermophilum var. thermophilum DSM 1495

UniProt G0RYI5

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 A; UniProt 1–462 Chain B; UniProt 1–462 Chain C; UniProt 1–462 Not recorded RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les2 × 1 (G0RY01) les6 × 1 (G0S590) Arp5 × 1 (G0S589) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0RYI5_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–462; UniProt 1–462 Author chain B; PDBConstruct 1–462; UniProt 1–462 Author chain C; PDBConstruct 1–462; UniProt 1–462

RuvB-like helicase

Chaetomium thermophilum var. thermophilum DSM 1495

UniProt G0RYC2

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 D; UniProt 1–488 Chain E; UniProt 1–488 Chain F; UniProt 1–488 Not recorded RuvB-like helicase × 3 (G0RYI5) Ino80 × 1 les2 × 1 (G0RY01) les6 × 1 (G0S590) Arp5 × 1 (G0S589) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0RYC2_CHATD
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–488; UniProt 1–488 Author chain E; PDBConstruct 1–488; UniProt 1–488 Author chain F; PDBConstruct 1–488; UniProt 1–488

les2

Chaetomium thermophilum var. thermophilum DSM 1495

UniProt G0RY01

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 H; UniProt 1–491 Not recorded RuvB-like helicase × 3 (G0RYI5) RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les6 × 1 (G0S590) Arp5 × 1 (G0S589) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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 G0RY01_CHATD
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–491; UniProt 1–491

les6

Chaetomium thermophilum var. thermophilum DSM 1495

UniProt G0S590

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 I; UniProt 1–219 Not recorded RuvB-like helicase × 3 (G0RYI5) RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les2 × 1 (G0RY01) Arp5 × 1 (G0S589) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S590_CHATD
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–219; UniProt 1–219

Arp5

Chaetomium thermophilum var. thermophilum DSM 1495

UniProt G0S589

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 J; UniProt 98–866 Not recorded RuvB-like helicase × 3 (G0RYI5) RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les2 × 1 (G0RY01) les6 × 1 (G0S590) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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.

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

View Construct and Data Evidence
UniProt name G0S589_CHATD
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–769; UniProt 98–866

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 6fhs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6fhs
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6fhs
Deposition date deposition_date2018-01-15
Structure title titleCryoEM Structure of INO80core
Keywords keywordsDNA 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_guinier51.18
Radius of gyration Rg (electron density) rg_electron50.90
Forward intensity I(0) i02229030000.00
Molecular weight molecular_weight390090.0 kDa
Excluded volume excluded_volume487470 ų
Envelope volume envelope_volume680500 ų
Hydration-shell volume shell_volume109980 ų
Envelope diameter envelope_diameter187.1
Shell Rg shell_rg55.93
Envelope Rg envelope_rg50.85
Shape Rg shape_rg50.96
Total Rg total_rg50.87
Total atoms total_atoms27383
Residues n_residues3510
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_real51.25
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real2.2290e+09
I(0) uncertainty (real space) i0_real_error4.5910e+07
Rg (reciprocal space) rg_reciprocal51.12
I(0) (reciprocal space) i0_reciprocal2229000000.0000
Solution quality estimate total_estimate0.8426
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.7
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis0.065
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha404700000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.760; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.672

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6fhsA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily360 — RuvBL1 DNA/RNA binding domain
Domain ID domain_id6fhsA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60
Domain ID domain_id6fhsB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily360 — RuvBL1 DNA/RNA binding domain
Domain ID domain_id6fhsB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60
Domain ID domain_id6fhsC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily360 — RuvBL1 DNA/RNA binding domain
Domain ID domain_id6fhsC02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60
Domain ID domain_id6fhsE01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60
Domain ID domain_id6fhsF01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60

8. Citations (1)

9. Files and Curves (10)