9fa7

Structure of the Integrator arm module containing subunits INTS10/13/14/15 (state 3)

Method: ELECTRON MICROSCOPY Dmax: 201.7 Å Quality: GOOD

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

Integrator complex subunit 15

Homo sapiens

UniProt Q96N11

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 1–449 Not recorded Integrator complex subunit 10 × 1 (Q9NVR2) Integrator complex subunit 13 × 1 (Q9NVM9) Integrator complex subunit 14 × 1 (Q96SY0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 INT15_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–449; UniProt 1–449

Integrator complex subunit 10

Homo sapiens

UniProt Q9NVR2

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 1–710 Not recorded Integrator complex subunit 15 × 1 (Q96N11) Integrator complex subunit 13 × 1 (Q9NVM9) Integrator complex subunit 14 × 1 (Q96SY0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 INT10_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–710; UniProt 1–710

Integrator complex subunit 13

Homo sapiens

UniProt Q9NVM9

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 1–706 Not recorded Integrator complex subunit 15 × 1 (Q96N11) Integrator complex subunit 10 × 1 (Q9NVR2) Integrator complex subunit 14 × 1 (Q96SY0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

9 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INT13_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–706; UniProt 1–706

Integrator complex subunit 14

Homo sapiens

UniProt Q96SY0

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 1–518 Not recorded Integrator complex subunit 15 × 1 (Q96N11) Integrator complex subunit 10 × 1 (Q9NVR2) Integrator complex subunit 13 × 1 (Q9NVM9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 INT14_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–518; UniProt 1–518

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 9fa7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fa7
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9fa7
Deposition date deposition_date2024-05-10
Structure title titleStructure of the Integrator arm module containing subunits INTS10/13/14/15 (state 3)
Keywords keywordsIntegrator complex assembly, RNA polymerase II transcription termination, transcription factors, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier69.57
Radius of gyration Rg (electron density) rg_electron69.98
Forward intensity I(0) i0601473000.00
Molecular weight molecular_weight209210.0 kDa
Excluded volume excluded_volume262910 ų
Envelope volume envelope_volume496280 ų
Hydration-shell volume shell_volume62152 ų
Envelope diameter envelope_diameter225.2
Shell Rg shell_rg66.66
Envelope Rg envelope_rg66.11
Shape Rg shape_rg69.97
Total Rg total_rg69.95
Total atoms total_atoms14712
Residues n_residues1961
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 dmax201.7
Rg (real space) rg_real69.83
Rg uncertainty (real space) rg_real_error1.48
I(0) (real space) i0_real6.0120e+08
I(0) uncertainty (real space) i0_real_error1.1510e+07
Rg (reciprocal space) rg_reciprocal68.12
I(0) (reciprocal space) i0_reciprocal599400000.0000
Solution quality estimate total_estimate0.7615
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.8
Skewness Skewness skewness0.243
Kurtosis Kurtosis kurtosis-1.032
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0027
Highest regularization parameter α highest_alpha13340000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.809; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.468; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)