7yfn

Core module of the NuA4 complex in S. cerevisiae

Method: ELECTRON MICROSCOPY Dmax: 188.8 Å Quality: REASONABLE

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

Actin

Saccharomyces cerevisiae

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 4–375 Not recorded ARP4 isoform 1 × 1 (A0A6A5PX31) Chromatin modification-related protein EAF1 × 1 (A0A8H8UNQ6) SWR1-complex protein 4 × 1 (A0A8H4F9Y4) Transcription-associated protein 1 × 1 (P38811) Enhancer of polycomb-like protein 1 × 1 (P43572) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–372; UniProt 4–375

ARP4 isoform 1

Saccharomyces cerevisiae

UniProt A0A6A5PX31

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 B; UniProt 1–489 Not recorded Actin × 1 (P60010) Chromatin modification-related protein EAF1 × 1 (A0A8H8UNQ6) SWR1-complex protein 4 × 1 (A0A8H4F9Y4) Transcription-associated protein 1 × 1 (P38811) Enhancer of polycomb-like protein 1 × 1 (P43572) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 A0A6A5PX31_YEASX
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–489; UniProt 1–489

Chromatin modification-related protein EAF1

Saccharomyces cerevisiae

UniProt A0A8H8UNQ6

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 D; UniProt 1–982 Not recorded Actin × 1 (P60010) ARP4 isoform 1 × 1 (A0A6A5PX31) SWR1-complex protein 4 × 1 (A0A8H4F9Y4) Transcription-associated protein 1 × 1 (P38811) Enhancer of polycomb-like protein 1 × 1 (P43572) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 A0A8H8UNQ6_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–982; UniProt 1–982

SWR1-complex protein 4

Saccharomyces cerevisiae

UniProt A0A8H4F9Y4

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 1–476 Not recorded Actin × 1 (P60010) ARP4 isoform 1 × 1 (A0A6A5PX31) Chromatin modification-related protein EAF1 × 1 (A0A8H8UNQ6) Transcription-associated protein 1 × 1 (P38811) Enhancer of polycomb-like protein 1 × 1 (P43572) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 A0A8H4F9Y4_YEASX
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–476; UniProt 1–476

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 T; UniProt 1–3744 Not recorded Actin × 1 (P60010) ARP4 isoform 1 × 1 (A0A6A5PX31) Chromatin modification-related protein EAF1 × 1 (A0A8H8UNQ6) SWR1-complex protein 4 × 1 (A0A8H4F9Y4) Enhancer of polycomb-like protein 1 × 1 (P43572) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 5
Chains and sequence ranges Author chain T; PDBConstruct 1–3744; UniProt 1–3744

Enhancer of polycomb-like protein 1

Saccharomyces cerevisiae

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 F; UniProt 1–832 Not recorded Actin × 1 (P60010) ARP4 isoform 1 × 1 (A0A6A5PX31) Chromatin modification-related protein EAF1 × 1 (A0A8H8UNQ6) SWR1-complex protein 4 × 1 (A0A8H4F9Y4) Transcription-associated protein 1 × 1 (P38811) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 6
Chains and sequence ranges Author chain F; PDBConstruct 1–832; UniProt 1–832

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 7yfn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7yfn
Deposition date deposition_date2022-07-08
Structure title titleCore module of the NuA4 complex in S. cerevisiae
Keywords keywordshistone, acetyltransferase, H4, NuA4, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.77
Radius of gyration Rg (electron density) rg_electron54.67
Forward intensity I(0) i01914250000.00
Molecular weight molecular_weight374110.0 kDa
Excluded volume excluded_volume471260 ų
Envelope volume envelope_volume681170 ų
Hydration-shell volume shell_volume103620 ų
Envelope diameter envelope_diameter202.0
Shell Rg shell_rg57.83
Envelope Rg envelope_rg53.58
Shape Rg shape_rg54.68
Total Rg total_rg54.75
Total atoms total_atoms26397
Residues n_residues3241
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 dmax188.8
Rg (real space) rg_real54.89
Rg uncertainty (real space) rg_real_error1.99
I(0) (real space) i0_real1.9140e+09
I(0) uncertainty (real space) i0_real_error4.1540e+07
Rg (reciprocal space) rg_reciprocal54.65
I(0) (reciprocal space) i0_reciprocal1914000000.0000
Solution quality estimate total_estimate0.6377
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary58.6
Skewness Skewness skewness0.405
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha321400000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 0.017; Positv: 1.000; Valcen: 0.999; Smooth: 0.769

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_id7yfnA01
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)