7v2w

protomer structure from the dimer of yeast THO complex

Method: ELECTRON MICROSCOPY Dmax: 201.6 Å Quality: GOOD

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

THO complex subunit HPR1

Saccharomyces cerevisiae S288c

UniProt P17629

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 1–752 Not recorded THO complex subunit 2 × 1 (P53552) Protein TEX1 × 1 (P53851) THO complex subunit MFT1 × 1 (P33441) THO complex subunit THP2 × 1 (O13539) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 HPR1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–752; UniProt 1–752

THO complex subunit 2

Saccharomyces cerevisiae S288c

UniProt P53552

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 1–1597 Not recorded THO complex subunit HPR1 × 1 (P17629) Protein TEX1 × 1 (P53851) THO complex subunit MFT1 × 1 (P33441) THO complex subunit THP2 × 1 (O13539) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THO2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–1597; UniProt 1–1597

Protein TEX1

Saccharomyces cerevisiae S288c

UniProt P53851

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 1–422 Not recorded THO complex subunit HPR1 × 1 (P17629) THO complex subunit 2 × 1 (P53552) THO complex subunit MFT1 × 1 (P33441) THO complex subunit THP2 × 1 (O13539) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TEX1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–422; UniProt 1–422

THO complex subunit MFT1

Saccharomyces cerevisiae S288c

UniProt P33441

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain I; UniProt 1–392 Not recorded THO complex subunit HPR1 × 1 (P17629) THO complex subunit 2 × 1 (P53552) Protein TEX1 × 1 (P53851) THO complex subunit THP2 × 1 (O13539) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 MFT1_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain I; PDBConstruct 1–392; UniProt 1–392

THO complex subunit THP2

Saccharomyces cerevisiae S288c

UniProt O13539

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain J; UniProt 1–261 Not recorded THO complex subunit HPR1 × 1 (P17629) THO complex subunit 2 × 1 (P53552) Protein TEX1 × 1 (P53851) THO complex subunit MFT1 × 1 (P33441) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THP2_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain J; PDBConstruct 1–261; UniProt 1–261

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 7v2w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v2w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v2w
Deposition date deposition_date2021-08-10
Structure title titleprotomer structure from the dimer of yeast THO complex
Keywords keywordsRNA transcription, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.87
Radius of gyration Rg (electron density) rg_electron62.36
Forward intensity I(0) i01283840000.00
Molecular weight molecular_weight306900.0 kDa
Excluded volume excluded_volume386950 ų
Envelope volume envelope_volume608810 ų
Hydration-shell volume shell_volume86441 ų
Envelope diameter envelope_diameter225.4
Shell Rg shell_rg56.52
Envelope Rg envelope_rg62.95
Shape Rg shape_rg62.33
Total Rg total_rg62.30
Total atoms total_atoms21619
Residues n_residues2655
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 dmax201.6
Rg (real space) rg_real62.55
Rg uncertainty (real space) rg_real_error1.80
I(0) (real space) i0_real1.2830e+09
I(0) uncertainty (real space) i0_real_error2.9050e+07
Rg (reciprocal space) rg_reciprocal61.19
I(0) (reciprocal space) i0_reciprocal1281000000.0000
Solution quality estimate total_estimate0.8120
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary193.6
Skewness Skewness skewness0.528
Kurtosis Kurtosis kurtosis-0.411
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0009
Highest regularization parameter α highest_alpha109100000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.108

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)