5y81

NuA4 TEEAA sub-complex

Method: ELECTRON MICROSCOPY Dmax: 214.7 Å Quality: GOOD

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

Transcription-associated protein 1

OrganismNot specified

UniProt P38811

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–2627 Chain B; UniProt 2630–3744 Fragment:UNP residues 2630-3744 Fragment:UNP residues 1-2627 Chromatin modification-related protein EAF1 × 1 (Q06337) Eaf1-disorder domain × 1 Chromatin modification-related protein EAF5 × 1 (P39995) Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) Chromatin modification-related protein EAF1 × 1 (Q06337) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRA1_YEAST
Isoform
PDB entities 1, 5
Chains and sequence ranges Author chain B; PDBConstruct 1–1115; UniProt 2630–3744 Author chain A; PDBConstruct 1–2627; UniProt 1–2627

Chromatin modification-related protein EAF1

OrganismNot specified

UniProt Q06337

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 647–982 Chain E; UniProt 357–397 Fragment:UNP residues 647-982 Fragment:UNP residues 357-397 Transcription-associated protein 1 × 1 (P38811) Eaf1-disorder domain × 1 Chromatin modification-related protein EAF5 × 1 (P39995) Transcription-associated protein 1 × 1 (P38811) Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EAF1_YEAST
Isoform
PDB entities 2, 8
Chains and sequence ranges Author chain C; PDBConstruct 2–336; UniProt 647–982 Author chain E; PDBConstruct 1–41; UniProt 357–397

Chromatin modification-related protein EAF5

OrganismNot specified

UniProt P39995

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain H; UniProt 1–279 Not recorded Transcription-associated protein 1 × 1 (P38811) Chromatin modification-related protein EAF1 × 1 (Q06337) Eaf1-disorder domain × 1 Transcription-associated protein 1 × 1 (P38811) Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) Chromatin modification-related protein EAF1 × 1 (Q06337) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name EAF5_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–279; UniProt 1–279

Actin-related protein 4

OrganismNot specified

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 1–489 Not recorded Transcription-associated protein 1 × 1 (P38811) Chromatin modification-related protein EAF1 × 1 (Q06337) Eaf1-disorder domain × 1 Chromatin modification-related protein EAF5 × 1 (P39995) Transcription-associated protein 1 × 1 (P38811) Actin × 1 (P60010) Chromatin modification-related protein EAF1 × 1 (Q06337) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 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 6
Chains and sequence ranges Author chain F; PDBConstruct 2–490; UniProt 1–489

Actin

OrganismNot specified

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 1–375 Not recorded Transcription-associated protein 1 × 1 (P38811) Chromatin modification-related protein EAF1 × 1 (Q06337) Eaf1-disorder domain × 1 Chromatin modification-related protein EAF5 × 1 (P39995) Transcription-associated protein 1 × 1 (P38811) Actin-related protein 4 × 1 (P80428) Chromatin modification-related protein EAF1 × 1 (Q06337) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 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 7
Chains and sequence ranges Author chain G; PDBConstruct 1–375; UniProt 1–375

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 5y81

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5y81
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5y81
Deposition date deposition_date2017-08-18
Structure title titleNuA4 TEEAA sub-complex
Keywords keywordsNuA4 complex, Histone acetyltransferases, Tra1/TRRAP, PIKK family, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier68.82
Radius of gyration Rg (electron density) rg_electron69.27
Forward intensity I(0) i02369650000.00
Molecular weight molecular_weight361480.0 kDa
Excluded volume excluded_volume430940 ų
Envelope volume envelope_volume939900 ų
Hydration-shell volume shell_volume119590 ų
Envelope diameter envelope_diameter233.6
Shell Rg shell_rg62.68
Envelope Rg envelope_rg67.60
Shape Rg shape_rg69.26
Total Rg total_rg69.15
Total atoms total_atoms25712
Residues n_residues4455
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 dmax214.7
Rg (real space) rg_real68.97
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real2.3700e+09
I(0) uncertainty (real space) i0_real_error5.2760e+07
Rg (reciprocal space) rg_reciprocal68.10
I(0) (reciprocal space) i0_reciprocal2366000000.0000
Solution quality estimate total_estimate0.8401
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary65.3
Skewness Skewness skewness0.374
Kurtosis Kurtosis kurtosis-0.510
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha213900000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.970; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.016

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)