8a5o

Structure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of S. cerevisiae INO80

Method: ELECTRON MICROSCOPY Dmax: 144.9 Å Quality: GOOD

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

Chromatin-remodeling ATPase INO80

Saccharomyces cerevisiae S288C

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 1–598 Not recorded Actin-like protein ARP8 × 1 (Q12386) Actin × 1 (P60010) Actin-related protein 4 × 1 (P80428) Ino eighty subunit 4 × 1 (Q08561) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE 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.

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 G; PDBConstruct 1–598; UniProt 1–598

Actin-like protein ARP8

Saccharomyces cerevisiae S288C

UniProt Q12386

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain U; UniProt 1–881 Not recorded Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin × 1 (P60010) Actin-related protein 4 × 1 (P80428) Ino eighty subunit 4 × 1 (Q08561) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE 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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP8_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain U; PDBConstruct 1–881; UniProt 1–881

Actin

Saccharomyces cerevisiae S288C

UniProt P60010

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain V; UniProt 1–375 Not recorded Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-like protein ARP8 × 1 (Q12386) Actin-related protein 4 × 1 (P80428) Ino eighty subunit 4 × 1 (Q08561) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE 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.

13 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACT_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain V; PDBConstruct 1–375; UniProt 1–375

Actin-related protein 4

Saccharomyces cerevisiae S288C

UniProt P80428

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain W; UniProt 1–489 Not recorded Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-like protein ARP8 × 1 (Q12386) Actin × 1 (P60010) Ino eighty subunit 4 × 1 (Q08561) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE 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.

10 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP4_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain W; PDBConstruct 1–489; UniProt 1–489

Ino eighty subunit 4

Saccharomyces cerevisiae S288C

UniProt Q08561

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain X; UniProt 1–116 Not recorded Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-like protein ARP8 × 1 (Q12386) Actin × 1 (P60010) Actin-related protein 4 × 1 (P80428) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IES4_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain X; PDBConstruct 1–116; UniProt 1–116

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 8a5o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8a5o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8a5o
Deposition date deposition_date2022-06-15
Structure title titleStructure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of S. cerevisiae INO80
Keywords keywordschromatin remodeler, INO80, Actin-related protein, 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_guinier40.98
Radius of gyration Rg (electron density) rg_electron40.70
Forward intensity I(0) i0474867000.00
Molecular weight molecular_weight178610.0 kDa
Excluded volume excluded_volume223640 ų
Envelope volume envelope_volume301410 ų
Hydration-shell volume shell_volume61676 ų
Envelope diameter envelope_diameter153.2
Shell Rg shell_rg46.01
Envelope Rg envelope_rg40.63
Shape Rg shape_rg40.70
Total Rg total_rg40.97
Total atoms total_atoms12571
Residues n_residues1555
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 dmax144.9
Rg (real space) rg_real41.06
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real4.7490e+08
I(0) uncertainty (real space) i0_real_error9.2840e+06
Rg (reciprocal space) rg_reciprocal40.98
I(0) (reciprocal space) i0_reciprocal474800000.0000
Solution quality estimate total_estimate0.8593
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.6
Skewness Skewness skewness0.414
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha120100000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.770; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.894; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8a5oV01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4

8. Citations (1)

9. Files and Curves (10)