9cae

Cryo-EM structure of the reconstituted RuvBL lobe of the human TIP60 complex (composite structure)

Method: ELECTRON MICROSCOPY Dmax: 183.6 Å Quality: GOOD

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

E1A-binding protein p400,E1A-binding protein p400/Haloalkane dehalogenase chimera

Rhodococcus rhodochrous

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain A; UniProt 658–3159 Not recorded Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2,RuvB-like 2/Maltose/maltodextrin-binding periplasmic protein chimera × 3 (Q9Y230) Actin, cytoplasmic 1 × 1 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–2503; UniProt 658–3159

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain B; UniProt 1–364 Not recorded E1A-binding protein p400,E1A-binding protein p400/Haloalkane dehalogenase chimera × 1 (Q96L91) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2,RuvB-like 2/Maltose/maltodextrin-binding periplasmic protein chimera × 3 (Q9Y230) Actin, cytoplasmic 1 × 1 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–364; UniProt 1–364

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain C; UniProt 359–620 Not recorded E1A-binding protein p400,E1A-binding protein p400/Haloalkane dehalogenase chimera × 1 (Q96L91) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2,RuvB-like 2/Maltose/maltodextrin-binding periplasmic protein chimera × 3 (Q9Y230) Actin, cytoplasmic 1 × 1 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 2–263; UniProt 359–620

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain E; UniProt 1–456 Chain G; UniProt 1–456 Chain I; UniProt 1–456 Not recorded E1A-binding protein p400,E1A-binding protein p400/Haloalkane dehalogenase chimera × 1 (Q96L91) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) RuvB-like 2,RuvB-like 2/Maltose/maltodextrin-binding periplasmic protein chimera × 3 (Q9Y230) Actin, cytoplasmic 1 × 1 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 4
Chains and sequence ranges Author chain E; PDBConstruct 1–456; UniProt 1–456 Author chain G; PDBConstruct 1–456; UniProt 1–456 Author chain I; PDBConstruct 1–456; UniProt 1–456

RuvB-like 2,RuvB-like 2/Maltose/maltodextrin-binding periplasmic protein chimera

Escherichia coli K-12

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain F; UniProt 1–463 Chain H; UniProt 1–463 Chain J; UniProt 1–463 Not recorded E1A-binding protein p400,E1A-binding protein p400/Haloalkane dehalogenase chimera × 1 (Q96L91) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) RuvB-like 1 × 3 (Q9Y265) Actin, cytoplasmic 1 × 1 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 5
Chains and sequence ranges Author chain F; PDBConstruct 1–463; UniProt 1–463 Author chain H; PDBConstruct 1–463; UniProt 1–463 Author chain J; PDBConstruct 1–463; UniProt 1–463

Actin, cytoplasmic 1

Homo sapiens

UniProt P60709

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain L; UniProt 1–375 Not recorded E1A-binding protein p400,E1A-binding protein p400/Haloalkane dehalogenase chimera × 1 (Q96L91) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2,RuvB-like 2/Maltose/maltodextrin-binding periplasmic protein chimera × 3 (Q9Y230) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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.

72 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain L; PDBConstruct 1–375; UniProt 1–375

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain M; UniProt 1–429 Not recorded E1A-binding protein p400,E1A-binding protein p400/Haloalkane dehalogenase chimera × 1 (Q96L91) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2,RuvB-like 2/Maltose/maltodextrin-binding periplasmic protein chimera × 3 (Q9Y230) Actin, cytoplasmic 1 × 1 (P60709) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 7
Chains and sequence ranges Author chain M; PDBConstruct 1–429; UniProt 1–429

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain N; UniProt 1–467 Not recorded E1A-binding protein p400,E1A-binding protein p400/Haloalkane dehalogenase chimera × 1 (Q96L91) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2,RuvB-like 2/Maltose/maltodextrin-binding periplasmic protein chimera × 3 (Q9Y230) Actin, cytoplasmic 1 × 1 (P60709) Actin-like protein 6A × 1 (O96019) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 8
Chains and sequence ranges Author chain N; PDBConstruct 1–467; UniProt 1–467

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 9cae

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9cae
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9cae
Deposition date deposition_date2024-06-17
Structure title titleCryo-EM structure of the reconstituted RuvBL lobe of the human TIP60 complex (composite structure)
Keywords keywordshistone acetyltransferase, chromatin regulator, transcription regulation, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.63
Radius of gyration Rg (electron density) rg_electron60.44
Forward intensity I(0) i03346660000.00
Molecular weight molecular_weight484890.0 kDa
Excluded volume excluded_volume606730 ų
Envelope volume envelope_volume888430 ų
Hydration-shell volume shell_volume122130 ų
Envelope diameter envelope_diameter197.1
Shell Rg shell_rg63.15
Envelope Rg envelope_rg58.99
Shape Rg shape_rg60.46
Total Rg total_rg60.43
Total atoms total_atoms34005
Residues n_residues4289
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 dmax183.6
Rg (real space) rg_real60.69
Rg uncertainty (real space) rg_real_error1.56
I(0) (real space) i0_real3.3470e+09
I(0) uncertainty (real space) i0_real_error6.7450e+07
Rg (reciprocal space) rg_reciprocal60.53
I(0) (reciprocal space) i0_reciprocal3346000000.0000
Solution quality estimate total_estimate0.8420
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.5
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.569
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha201400000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.978; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.008

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)