8r22

INTS9-INTS11-BRAT1-WDR73 complex

Method: ELECTRON MICROSCOPY Dmax: 134.6 Å Quality: EXCELLENT

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

BRCA1-associated ATM activator 1

Homo sapiens

UniProt Q6PJG6

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–821 Not recorded Integrator complex subunit 9 × 1 (Q9NV88) Integrator complex subunit 11 × 1 (Q5TA45) WD repeat-containing protein 73 × 1 (Q6P4I2) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.90 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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BRAT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–827; UniProt 1–821

Integrator complex subunit 9

Homo sapiens

UniProt Q9NV88

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–658 Not recorded BRCA1-associated ATM activator 1 × 1 (Q6PJG6) Integrator complex subunit 11 × 1 (Q5TA45) WD repeat-containing protein 73 × 1 (Q6P4I2) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.90 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.

14 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INT9_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–658; UniProt 1–658

Integrator complex subunit 11

Homo sapiens

UniProt Q5TA45

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–600 Not recorded BRCA1-associated ATM activator 1 × 1 (Q6PJG6) Integrator complex subunit 9 × 1 (Q9NV88) WD repeat-containing protein 73 × 1 (Q6P4I2) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.90 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.

14 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INT11_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 13–612; UniProt 1–600

WD repeat-containing protein 73

Homo sapiens

UniProt Q6P4I2

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–378 Not recorded BRCA1-associated ATM activator 1 × 1 (Q6PJG6) Integrator complex subunit 9 × 1 (Q9NV88) Integrator complex subunit 11 × 1 (Q5TA45) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.90 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name WDR73_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 8–385; UniProt 1–378

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 8r22

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r22
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8r22
Deposition date deposition_date2023-11-02
Structure title titleINTS9-INTS11-BRAT1-WDR73 complex
Keywords keywordsChaperone, nuclear import, Integrator complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.34
Radius of gyration Rg (electron density) rg_electron41.75
Forward intensity I(0) i0662378000.00
Molecular weight molecular_weight214520.0 kDa
Excluded volume excluded_volume269630 ų
Envelope volume envelope_volume368210 ų
Hydration-shell volume shell_volume72372 ų
Envelope diameter envelope_diameter138.4
Shell Rg shell_rg48.31
Envelope Rg envelope_rg41.32
Shape Rg shape_rg41.77
Total Rg total_rg42.01
Total atoms total_atoms15069
Residues n_residues1950
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 dmax134.6
Rg (real space) rg_real42.19
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real6.6240e+08
I(0) uncertainty (real space) i0_real_error1.0550e+07
Rg (reciprocal space) rg_reciprocal42.34
I(0) (reciprocal space) i0_reciprocal662500000.0000
Solution quality estimate total_estimate0.9018
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.6
Skewness Skewness skewness0.175
Kurtosis Kurtosis kurtosis-0.559
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha138500000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.917

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)