8esc

Structure of the Yeast NuA4 Histone Acetyltransferase Complex

Method: ELECTRON MICROSCOPY Dmax: 261.7 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain Z; UniProt 1–3744 Not recorded Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) Enhancer of polycomb-like protein 1 × 1 (P43572) Chromatin modification-related protein EAF1 × 1 (Q06337) SWR1-complex protein 4 × 1 (P53201) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE 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 1
Chains and sequence ranges Author chain Z; PDBConstruct 1–3744; UniProt 1–3744

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain R; UniProt 1–489 Not recorded Transcription-associated protein 1 × 1 (P38811) Actin × 1 (P60010) Enhancer of polycomb-like protein 1 × 1 (P43572) Chromatin modification-related protein EAF1 × 1 (Q06337) SWR1-complex protein 4 × 1 (P53201) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE 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 R; PDBConstruct 1–489; 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–375 Not recorded Transcription-associated protein 1 × 1 (P38811) Actin-related protein 4 × 1 (P80428) Enhancer of polycomb-like protein 1 × 1 (P43572) Chromatin modification-related protein EAF1 × 1 (Q06337) SWR1-complex protein 4 × 1 (P53201) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE 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 A; PDBConstruct 1–375; UniProt 1–375

Enhancer of polycomb-like protein 1

OrganismNot specified

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 P; UniProt 1–832 Not recorded Transcription-associated protein 1 × 1 (P38811) Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) Chromatin modification-related protein EAF1 × 1 (Q06337) SWR1-complex protein 4 × 1 (P53201) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE 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 4
Chains and sequence ranges Author chain P; PDBConstruct 1–832; UniProt 1–832

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–982 Not recorded Transcription-associated protein 1 × 1 (P38811) Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) Enhancer of polycomb-like protein 1 × 1 (P43572) SWR1-complex protein 4 × 1 (P53201) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE 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 5
Chains and sequence ranges Author chain E; PDBConstruct 1–982; UniProt 1–982

SWR1-complex protein 4

OrganismNot specified

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 S; UniProt 1–476 Not recorded Transcription-associated protein 1 × 1 (P38811) Actin-related protein 4 × 1 (P80428) Actin × 1 (P60010) Enhancer of polycomb-like protein 1 × 1 (P43572) Chromatin modification-related protein EAF1 × 1 (Q06337) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE 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 6
Chains and sequence ranges Author chain S; PDBConstruct 1–476; UniProt 1–476

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 8esc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8esc
Deposition date deposition_date2022-10-13
Structure title titleStructure of the Yeast NuA4 Histone Acetyltransferase Complex
Keywords keywordsHistone Acetyltransferase, NuA4, Yeast, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier70.41
Radius of gyration Rg (electron density) rg_electron70.59
Forward intensity I(0) i04894860000.00
Molecular weight molecular_weight613750.0 kDa
Excluded volume excluded_volume777050 ų
Envelope volume envelope_volume1196500 ų
Hydration-shell volume shell_volume145360 ų
Envelope diameter envelope_diameter237.1
Shell Rg shell_rg67.06
Envelope Rg envelope_rg69.14
Shape Rg shape_rg70.59
Total Rg total_rg70.54
Total atoms total_atoms43279
Residues n_residues5300
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 dmax261.7
Rg (real space) rg_real70.79
Rg uncertainty (real space) rg_real_error2.70
I(0) (real space) i0_real4.8980e+09
I(0) uncertainty (real space) i0_real_error1.1930e+08
Rg (reciprocal space) rg_reciprocal69.69
I(0) (reciprocal space) i0_reciprocal4886000000.0000
Solution quality estimate total_estimate0.8459
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.4
Skewness Skewness skewness0.418
Kurtosis Kurtosis kurtosis-0.400
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0365
Highest regularization parameter α highest_alpha381100000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.729; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.803

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_id8escA01
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)