5l3t

Structure of the Saccharomyces cerevisiae TREX-2 complex

Method: X-RAY DIFFRACTION Dmax: 110.5 Å Quality: GOOD

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

Nuclear mRNA export protein SAC3

Saccharomyces cerevisiae

UniProt P46674

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–1301 Not recorded Nuclear mRNA export protein THP1 × 1 (Q08231) 26S proteasome complex subunit SEM1 × 1 (O94742) Sac3polyAla × 2 Sac3polyAla × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Precipitant: 20% PEG 3350, 0.2 M Mg formate; protein 16.5 mg/ml in 0.3 M NaCl, 50 mM HEPES, pH 8, 5 mM DTT. Resolution 4.93 Å R-free 0.370

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAC3_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1301; UniProt 1–1301

Nuclear mRNA export protein THP1

Saccharomyces cerevisiae

UniProt Q08231

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–455 Not recorded Nuclear mRNA export protein SAC3 × 1 (P46674) 26S proteasome complex subunit SEM1 × 1 (O94742) Sac3polyAla × 2 Sac3polyAla × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Precipitant: 20% PEG 3350, 0.2 M Mg formate; protein 16.5 mg/ml in 0.3 M NaCl, 50 mM HEPES, pH 8, 5 mM DTT. Resolution 4.93 Å R-free 0.370

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THP1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–455; UniProt 1–455

26S proteasome complex subunit SEM1

Saccharomyces cerevisiae

UniProt O94742

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–89 Not recorded Nuclear mRNA export protein SAC3 × 1 (P46674) Nuclear mRNA export protein THP1 × 1 (Q08231) Sac3polyAla × 2 Sac3polyAla × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Precipitant: 20% PEG 3350, 0.2 M Mg formate; protein 16.5 mg/ml in 0.3 M NaCl, 50 mM HEPES, pH 8, 5 mM DTT. Resolution 4.93 Å R-free 0.370

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.

35 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEM1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–89; UniProt 1–89

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 5l3t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5l3t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5l3t
Deposition date deposition_date2016-05-24
Structure title titleStructure of the Saccharomyces cerevisiae TREX-2 complex
Keywords keywordsnuclear export, TREX-2 complex, Sac3, Thp1, transport protein; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.97
Radius of gyration Rg (electron density) rg_electron32.08
Forward intensity I(0) i0142789000.00
Molecular weight molecular_weight96834.0 kDa
Excluded volume excluded_volume121780 ų
Envelope volume envelope_volume154930 ų
Hydration-shell volume shell_volume40256 ų
Envelope diameter envelope_diameter110.9
Shell Rg shell_rg38.71
Envelope Rg envelope_rg32.61
Shape Rg shape_rg32.07
Total Rg total_rg32.63
Total atoms total_atoms6831
Residues n_residues849
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 dmax110.5
Rg (real space) rg_real32.98
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real1.4280e+08
I(0) uncertainty (real space) i0_real_error2.4320e+06
Rg (reciprocal space) rg_reciprocal32.98
I(0) (reciprocal space) i0_reciprocal142800000.0000
Solution quality estimate total_estimate0.8164
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.8
Skewness Skewness skewness0.320
Kurtosis Kurtosis kurtosis-0.458
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40150000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)