8qri

TRRAP and EP400 in the human Tip60 complex

Method: ELECTRON MICROSCOPY Dmax: 197.6 Å Quality: GOOD

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

Transformation/transcription domain-associated protein

OrganismNot specified

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–3859 Not recorded E1A-binding protein p400 × 1 (Q96L91) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–3859; UniProt 1–3859

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–3159 Not recorded Transformation/transcription domain-associated protein × 1 (Q9Y4A5) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–3159; UniProt 1–3159

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 8qri

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8qri
Deposition date deposition_date2023-10-09
Structure title titleTRRAP and EP400 in the human Tip60 complex
Keywords keywordsEukaryotic transcription, Histone acetyltransferase, chromatin remodeling, Complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.64
Radius of gyration Rg (electron density) rg_electron57.62
Forward intensity I(0) i01976400000.00
Molecular weight molecular_weight387320.0 kDa
Excluded volume excluded_volume490880 ų
Envelope volume envelope_volume762990 ų
Hydration-shell volume shell_volume108430 ų
Envelope diameter envelope_diameter190.9
Shell Rg shell_rg62.63
Envelope Rg envelope_rg56.20
Shape Rg shape_rg57.63
Total Rg total_rg57.71
Total atoms total_atoms55049
Residues n_residues3380
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 dmax197.6
Rg (real space) rg_real57.65
Rg uncertainty (real space) rg_real_error1.84
I(0) (real space) i0_real1.9760e+09
I(0) uncertainty (real space) i0_real_error3.9350e+07
Rg (reciprocal space) rg_reciprocal57.60
I(0) (reciprocal space) i0_reciprocal1976000000.0000
Solution quality estimate total_estimate0.8155
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary65.9
Skewness Skewness skewness0.308
Kurtosis Kurtosis kurtosis-0.481
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha158800000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)