9eof

Structure of the human INTS5/8/10/15 subcomplex

Method: ELECTRON MICROSCOPY Dmax: 231.4 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 8 × 1 (Q75QN2) Integrator complex subunit 5 × 1 (Q6P9B9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.70 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 8 × 1 (Q75QN2) Integrator complex subunit 5 × 1 (Q6P9B9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.70 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 8

Homo sapiens

UniProt Q75QN2

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 F; UniProt 1–995 Not recorded Integrator complex subunit 15 × 1 (Q96N11) Integrator complex subunit 10 × 1 (Q9NVR2) Integrator complex subunit 5 × 1 (Q6P9B9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.70 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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INT8_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 1–995; UniProt 1–995

Integrator complex subunit 5

Homo sapiens

UniProt Q6P9B9

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 G; UniProt 1–1019 Not recorded Integrator complex subunit 15 × 1 (Q96N11) Integrator complex subunit 10 × 1 (Q9NVR2) Integrator complex subunit 8 × 1 (Q75QN2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.70 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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INT5_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–1019; UniProt 1–1019

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 9eof

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9eof
Deposition date deposition_date2024-03-14
Structure title titleStructure of the human INTS5/8/10/15 subcomplex
Keywords keywordsIntegrator complex, 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_guinier87.35
Radius of gyration Rg (electron density) rg_electron89.17
Forward intensity I(0) i01048870000.00
Molecular weight molecular_weight278130.0 kDa
Excluded volume excluded_volume349710 ų
Envelope volume envelope_volume686240 ų
Hydration-shell volume shell_volume70967 ų
Envelope diameter envelope_diameter306.5
Shell Rg shell_rg70.93
Envelope Rg envelope_rg87.36
Shape Rg shape_rg89.21
Total Rg total_rg88.75
Total atoms total_atoms19577
Residues n_residues2613
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 dmax231.4
Rg (real space) rg_real81.01
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real9.9960e+08
I(0) uncertainty (real space) i0_real_error2.0880e+07
Rg (reciprocal space) rg_reciprocal80.68
I(0) (reciprocal space) i0_reciprocal1029000000.0000
Solution quality estimate total_estimate0.8430
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.4
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.951
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.7294
Highest regularization parameter α highest_alpha24130000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.822; Stabil: 0.954; Sysdev: 1.000; Positv: 1.000; Valcen: 0.634; 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)