9c62

P400 subcomplex of the native human TIP60 complex

Method: ELECTRON MICROSCOPY Dmax: 224.1 Å Quality: GOOD

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

RuvB-like 2

OrganismNot specified

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain B; UniProt 1–463 Chain D; UniProt 1–463 Chain F; UniProt 1–463 Not recorded RuvB-like 1 × 3 (Q9Y265) E1A-binding protein p400 × 1 (Q96L91) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Actin, cytoplasmic 1 × 1 (P60709) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-like protein 6A × 2 (O96019) Histone H2A.Z × 1 (P0C0S5) Histone H2B type 1-B × 1 (P33778) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.28 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 1
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

RuvB-like 1

OrganismNot specified

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 1–456 Chain C; UniProt 1–456 Chain E; UniProt 1–456 Not recorded RuvB-like 2 × 3 (Q9Y230) E1A-binding protein p400 × 1 (Q96L91) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Actin, cytoplasmic 1 × 1 (P60709) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-like protein 6A × 2 (O96019) Histone H2A.Z × 1 (P0C0S5) Histone H2B type 1-B × 1 (P33778) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.28 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

E1A-binding protein p400

OrganismNot specified

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain G; UniProt 1–3159 Not recorded RuvB-like 2 × 3 (Q9Y230) RuvB-like 1 × 3 (Q9Y265) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Actin, cytoplasmic 1 × 1 (P60709) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-like protein 6A × 2 (O96019) Histone H2A.Z × 1 (P0C0S5) Histone H2B type 1-B × 1 (P33778) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.28 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 3
Chains and sequence ranges Author chain G; PDBConstruct 1–3159; UniProt 1–3159

Enhancer of polycomb homolog 1

OrganismNot specified

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain H; UniProt 1–836 Not recorded RuvB-like 2 × 3 (Q9Y230) RuvB-like 1 × 3 (Q9Y265) E1A-binding protein p400 × 1 (Q96L91) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Actin, cytoplasmic 1 × 1 (P60709) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-like protein 6A × 2 (O96019) Histone H2A.Z × 1 (P0C0S5) Histone H2B type 1-B × 1 (P33778) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.28 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 4
Chains and sequence ranges Author chain H; PDBConstruct 1–836; UniProt 1–836

DNA methyltransferase 1-associated protein 1

OrganismNot specified

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain I; UniProt 1–467 Not recorded RuvB-like 2 × 3 (Q9Y230) RuvB-like 1 × 3 (Q9Y265) E1A-binding protein p400 × 1 (Q96L91) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) Actin, cytoplasmic 1 × 1 (P60709) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-like protein 6A × 2 (O96019) Histone H2A.Z × 1 (P0C0S5) Histone H2B type 1-B × 1 (P33778) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.28 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 5
Chains and sequence ranges Author chain I; PDBConstruct 1–467; UniProt 1–467

Actin, cytoplasmic 1

OrganismNot specified

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain J; UniProt 1–375 Not recorded RuvB-like 2 × 3 (Q9Y230) RuvB-like 1 × 3 (Q9Y265) E1A-binding protein p400 × 1 (Q96L91) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-like protein 6A × 2 (O96019) Histone H2A.Z × 1 (P0C0S5) Histone H2B type 1-B × 1 (P33778) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.28 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 J; PDBConstruct 1–375; UniProt 1–375

Vacuolar protein sorting-associated protein 72 homolog

OrganismNot specified

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain K; UniProt 1–364 Not recorded RuvB-like 2 × 3 (Q9Y230) RuvB-like 1 × 3 (Q9Y265) E1A-binding protein p400 × 1 (Q96L91) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Actin, cytoplasmic 1 × 1 (P60709) Actin-like protein 6A × 2 (O96019) Histone H2A.Z × 1 (P0C0S5) Histone H2B type 1-B × 1 (P33778) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.28 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 7
Chains and sequence ranges Author chain K; PDBConstruct 1–364; UniProt 1–364

Actin-like protein 6A

OrganismNot specified

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain L; UniProt 1–429 Chain M; UniProt 1–429 Not recorded RuvB-like 2 × 3 (Q9Y230) RuvB-like 1 × 3 (Q9Y265) E1A-binding protein p400 × 1 (Q96L91) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Actin, cytoplasmic 1 × 1 (P60709) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Histone H2A.Z × 1 (P0C0S5) Histone H2B type 1-B × 1 (P33778) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.28 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 8
Chains and sequence ranges Author chain L; PDBConstruct 1–429; UniProt 1–429 Author chain M; PDBConstruct 1–429; UniProt 1–429

Histone H2A.Z

OrganismNot specified

UniProt P0C0S5

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain N; UniProt 1–128 Not recorded RuvB-like 2 × 3 (Q9Y230) RuvB-like 1 × 3 (Q9Y265) E1A-binding protein p400 × 1 (Q96L91) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Actin, cytoplasmic 1 × 1 (P60709) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-like protein 6A × 2 (O96019) Histone H2B type 1-B × 1 (P33778) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.28 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.

25 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2AZ_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain N; PDBConstruct 1–128; UniProt 1–128

Histone H2B type 1-B

OrganismNot specified

UniProt P33778

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain O; UniProt 1–126 Not recorded RuvB-like 2 × 3 (Q9Y230) RuvB-like 1 × 3 (Q9Y265) E1A-binding protein p400 × 1 (Q96L91) Enhancer of polycomb homolog 1 × 1 (Q9H2F5) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) Actin, cytoplasmic 1 × 1 (P60709) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-like protein 6A × 2 (O96019) Histone H2A.Z × 1 (P0C0S5) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.28 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1B_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain O; PDBConstruct 1–126; UniProt 1–126

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 9c62

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c62
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c62
Deposition date deposition_date2024-06-07
Structure title titleP400 subcomplex of the native human TIP60 complex
Keywords keywordscomplex, chromatin regulator, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.90
Radius of gyration Rg (electron density) rg_electron67.63
Forward intensity I(0) i04428340000.00
Molecular weight molecular_weight561900.0 kDa
Excluded volume excluded_volume703910 ų
Envelope volume envelope_volume1128300 ų
Hydration-shell volume shell_volume138990 ų
Envelope diameter envelope_diameter216.6
Shell Rg shell_rg68.76
Envelope Rg envelope_rg65.21
Shape Rg shape_rg67.66
Total Rg total_rg67.51
Total atoms total_atoms79168
Residues n_residues4997
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 dmax224.1
Rg (real space) rg_real67.80
Rg uncertainty (real space) rg_real_error2.21
I(0) (real space) i0_real4.4280e+09
I(0) uncertainty (real space) i0_real_error9.5810e+07
Rg (reciprocal space) rg_reciprocal68.08
I(0) (reciprocal space) i0_reciprocal4430000000.0000
Solution quality estimate total_estimate0.8714
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary68.2
Skewness Skewness skewness0.150
Kurtosis Kurtosis kurtosis-0.734
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha317600000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.597

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)