7vvy

TRA module of NuA4

Method: ELECTRON MICROSCOPY Dmax: 263.1 Å Quality: GOOD

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

Chromatin modification-related protein EAF1

Saccharomyces cerevisiae S288C

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–982 Not recorded Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) SWR1-complex protein 4 × 1 (P53201) Enhancer of polycomb-like protein 1 × 1 (P43572) Transcription-associated protein 1 × 1 (P38811) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.10 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 1
Chains and sequence ranges Author chain E; PDBConstruct 1–982; UniProt 1–982

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 1–489 Not recorded Chromatin modification-related protein EAF1 × 1 (Q06337) Actin × 1 (P60010) SWR1-complex protein 4 × 1 (P53201) Enhancer of polycomb-like protein 1 × 1 (P43572) Transcription-associated protein 1 × 1 (P38811) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.10 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 2
Chains and sequence ranges Author chain F; PDBConstruct 1–489; UniProt 1–489

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 1–375 Not recorded Chromatin modification-related protein EAF1 × 1 (Q06337) Actin-related protein 4 × 1 (P80428) SWR1-complex protein 4 × 1 (P53201) Enhancer of polycomb-like protein 1 × 1 (P43572) Transcription-associated protein 1 × 1 (P38811) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.10 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 G; PDBConstruct 1–375; UniProt 1–375

SWR1-complex protein 4

Saccharomyces cerevisiae S288C

UniProt P53201

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain K; UniProt 1–476 Not recorded Chromatin modification-related protein EAF1 × 1 (Q06337) Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) Enhancer of polycomb-like protein 1 × 1 (P43572) Transcription-associated protein 1 × 1 (P38811) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.10 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SWC4_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 1–476; UniProt 1–476

Enhancer of polycomb-like protein 1

Saccharomyces cerevisiae S288C

UniProt P43572

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain H; UniProt 1–832 Not recorded Chromatin modification-related protein EAF1 × 1 (Q06337) Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) SWR1-complex protein 4 × 1 (P53201) Transcription-associated protein 1 × 1 (P38811) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.10 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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EPL1_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain H; PDBConstruct 1–832; UniProt 1–832

Transcription-associated protein 1

Saccharomyces cerevisiae

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain L; UniProt 1–3744 Not recorded Chromatin modification-related protein EAF1 × 1 (Q06337) Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) SWR1-complex protein 4 × 1 (P53201) Enhancer of polycomb-like protein 1 × 1 (P43572) MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.10 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 6
Chains and sequence ranges Author chain L; PDBConstruct 1–3744; UniProt 1–3744

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 7vvy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7vvy
Deposition date deposition_date2021-11-09
Structure title titleTRA module of NuA4
Keywords keywordsNuA4 Tra1, 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_guinier70.79
Radius of gyration Rg (electron density) rg_electron71.05
Forward intensity I(0) i04727620000.00
Molecular weight molecular_weight603380.0 kDa
Excluded volume excluded_volume764080 ų
Envelope volume envelope_volume1207900 ų
Hydration-shell volume shell_volume146140 ų
Envelope diameter envelope_diameter240.9
Shell Rg shell_rg67.08
Envelope Rg envelope_rg69.60
Shape Rg shape_rg71.05
Total Rg total_rg71.01
Total atoms total_atoms42546
Residues n_residues5205
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 dmax263.1
Rg (real space) rg_real71.07
Rg uncertainty (real space) rg_real_error2.72
I(0) (real space) i0_real4.7290e+09
I(0) uncertainty (real space) i0_real_error1.0290e+08
Rg (reciprocal space) rg_reciprocal70.06
I(0) (reciprocal space) i0_reciprocal4719000000.0000
Solution quality estimate total_estimate0.8473
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.8
Skewness Skewness skewness0.411
Kurtosis Kurtosis kurtosis-0.418
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0173
Highest regularization parameter α highest_alpha353200000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.731; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.818

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7vvyG01
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)