8xvg

Structure of human NuA4/TIP60 complex

Method: ELECTRON MICROSCOPY Dmax: 259.7 Å Quality: EXCELLENT

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

Isoform 2 of Transformation/transcription domain-associated protein

Homo sapiens

UniProt Q9Y4A5

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain L; UniProt 1–3830 Not recorded RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Isoform 2 of E1A-binding protein p400 × 1 (Q96L91) Actin-like protein 6A × 2 (O96019) ACTB protein (Fragment) × 1 (A0A7K5XZZ2) Isoform 2 of Enhancer of polycomb homolog 1 × 1 (Q9H2F5) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) IHP INOSITOL HEXAKISPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRRAP_HUMAN
Isoform Q9Y4A5-2
PDB entities 1
Chains and sequence ranges Author chain L; PDBConstruct 1–3830; UniProt 1–3830

RuvB-like 1

Homo sapiens

UniProt Q9Y265

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain A; UniProt 1–456 Chain C; UniProt 1–456 Chain E; UniProt 1–456 Not recorded Isoform 2 of Transformation/transcription domain-associated protein × 1 (Q9Y4A5) RuvB-like 2 × 3 (Q9Y230) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Isoform 2 of E1A-binding protein p400 × 1 (Q96L91) Actin-like protein 6A × 2 (O96019) ACTB protein (Fragment) × 1 (A0A7K5XZZ2) Isoform 2 of Enhancer of polycomb homolog 1 × 1 (Q9H2F5) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) IHP INOSITOL HEXAKISPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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.

35 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUVB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–456; UniProt 1–456 Author chain C; PDBConstruct 1–456; UniProt 1–456 Author chain E; PDBConstruct 1–456; UniProt 1–456

RuvB-like 2

Homo sapiens

UniProt Q9Y230

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain B; UniProt 1–463 Chain D; UniProt 1–463 Chain F; UniProt 1–463 Not recorded Isoform 2 of Transformation/transcription domain-associated protein × 1 (Q9Y4A5) RuvB-like 1 × 3 (Q9Y265) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Isoform 2 of E1A-binding protein p400 × 1 (Q96L91) Actin-like protein 6A × 2 (O96019) ACTB protein (Fragment) × 1 (A0A7K5XZZ2) Isoform 2 of Enhancer of polycomb homolog 1 × 1 (Q9H2F5) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) IHP INOSITOL HEXAKISPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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.

37 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUVB2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–463; UniProt 1–463 Author chain D; PDBConstruct 1–463; UniProt 1–463 Author chain F; PDBConstruct 1–463; UniProt 1–463

DNA methyltransferase 1-associated protein 1

Homo sapiens

UniProt Q9NPF5

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain G; UniProt 1–467 Not recorded Isoform 2 of Transformation/transcription domain-associated protein × 1 (Q9Y4A5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Isoform 2 of E1A-binding protein p400 × 1 (Q96L91) Actin-like protein 6A × 2 (O96019) ACTB protein (Fragment) × 1 (A0A7K5XZZ2) Isoform 2 of Enhancer of polycomb homolog 1 × 1 (Q9H2F5) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) IHP INOSITOL HEXAKISPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DMAP1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–467; UniProt 1–467

Isoform 2 of E1A-binding protein p400

Homo sapiens

UniProt Q96L91

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain H; UniProt 1–3123 Not recorded Isoform 2 of Transformation/transcription domain-associated protein × 1 (Q9Y4A5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Actin-like protein 6A × 2 (O96019) ACTB protein (Fragment) × 1 (A0A7K5XZZ2) Isoform 2 of Enhancer of polycomb homolog 1 × 1 (Q9H2F5) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) IHP INOSITOL HEXAKISPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EP400_HUMAN
Isoform Q96L91-2
PDB entities 5
Chains and sequence ranges Author chain H; PDBConstruct 1–3123; UniProt 1–3123

Actin-like protein 6A

Homo sapiens

UniProt O96019

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain I; UniProt 1–429 Chain J; UniProt 1–429 Not recorded Isoform 2 of Transformation/transcription domain-associated protein × 1 (Q9Y4A5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Isoform 2 of E1A-binding protein p400 × 1 (Q96L91) ACTB protein (Fragment) × 1 (A0A7K5XZZ2) Isoform 2 of Enhancer of polycomb homolog 1 × 1 (Q9H2F5) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) IHP INOSITOL HEXAKISPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACL6A_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain I; PDBConstruct 1–429; UniProt 1–429 Author chain J; PDBConstruct 1–429; UniProt 1–429

ACTB protein (Fragment)

Homo sapiens

UniProt A0A7K5XZZ2

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain K; UniProt 1–375 Not recorded Isoform 2 of Transformation/transcription domain-associated protein × 1 (Q9Y4A5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Isoform 2 of E1A-binding protein p400 × 1 (Q96L91) Actin-like protein 6A × 2 (O96019) Isoform 2 of Enhancer of polycomb homolog 1 × 1 (Q9H2F5) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) IHP INOSITOL HEXAKISPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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 A0A7K5XZZ2_9CHAR
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–375; UniProt 1–375

Isoform 2 of Enhancer of polycomb homolog 1

Homo sapiens

UniProt Q9H2F5

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain M; UniProt 1–813 Not recorded Isoform 2 of Transformation/transcription domain-associated protein × 1 (Q9Y4A5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Isoform 2 of E1A-binding protein p400 × 1 (Q96L91) Actin-like protein 6A × 2 (O96019) ACTB protein (Fragment) × 1 (A0A7K5XZZ2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) IHP INOSITOL HEXAKISPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EPC1_HUMAN
Isoform Q9H2F5-2
PDB entities 8
Chains and sequence ranges Author chain M; PDBConstruct 1–813; UniProt 1–813

Vacuolar protein sorting-associated protein 72 homolog

Homo sapiens

UniProt Q15906

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain N; UniProt 1–364 Not recorded Isoform 2 of Transformation/transcription domain-associated protein × 1 (Q9Y4A5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Isoform 2 of E1A-binding protein p400 × 1 (Q96L91) Actin-like protein 6A × 2 (O96019) ACTB protein (Fragment) × 1 (A0A7K5XZZ2) Isoform 2 of Enhancer of polycomb homolog 1 × 1 (Q9H2F5) IHP INOSITOL HEXAKISPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS72_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain N; PDBConstruct 1–364; UniProt 1–364

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 8xvg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8xvg
Deposition date deposition_date2024-01-15
Structure title titleStructure of human NuA4/TIP60 complex
Keywords keywordsRemodeler; Histone Acetyltransferase Complex; NuA4; TIP60, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron101.70
Forward intensity I(0) i012720500000.00
Molecular weight molecular_weight973690.0 kDa
Excluded volume excluded_volume1223900 ų
Envelope volume envelope_volume2144900 ų
Hydration-shell volume shell_volume174060 ų
Envelope diameter envelope_diameter328.6
Shell Rg shell_rg97.17
Envelope Rg envelope_rg97.31
Shape Rg shape_rg101.70
Total Rg total_rg101.70
Total atoms total_atoms98226
Residues n_residues8571
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 dmax259.7
Rg (real space) rg_real96.91
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.2180e+10
I(0) uncertainty (real space) i0_real_error2.5050e+08
Rg (reciprocal space) rg_reciprocal96.36
I(0) (reciprocal space) i0_reciprocal12520000000.0000
Solution quality estimate total_estimate0.9103
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary86.6
Skewness Skewness skewness0.200
Kurtosis Kurtosis kurtosis-0.962
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.9418
Highest regularization parameter α highest_alpha314000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.998; Stabil: 0.956; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)