4trq

Crystal structure of Sac3/Thp1/Sem1

Method: X-RAY DIFFRACTION Dmax: 124.0 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 253–551 Chain D; UniProt 253–551 Not recorded Nuclear mRNA export protein THP1 × 2 (Q08231) 26S proteasome complex subunit SEM1 × 2 (O94742) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.5M Li2SO4, 10% PEG-8.000 Resolution 3.10 Å R-free 0.238

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 1–299; UniProt 253–551 Author chain D; PDBConstruct 1–299; UniProt 253–551

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 170–455 Chain E; UniProt 170–455 Not recorded Nuclear mRNA export protein SAC3 × 2 (P46674) 26S proteasome complex subunit SEM1 × 2 (O94742) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.5M Li2SO4, 10% PEG-8.000 Resolution 3.10 Å R-free 0.238

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 1–286; UniProt 170–455 Author chain E; PDBConstruct 1–286; UniProt 170–455

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 30–89 Chain F; UniProt 30–89 Not recorded Nuclear mRNA export protein SAC3 × 2 (P46674) Nuclear mRNA export protein THP1 × 2 (Q08231) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.5M Li2SO4, 10% PEG-8.000 Resolution 3.10 Å R-free 0.238

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 1–60; UniProt 30–89 Author chain F; PDBConstruct 1–60; UniProt 30–89

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 4trq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4trq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4trq
Deposition date deposition_date2014-06-17
Structure title titleCrystal structure of Sac3/Thp1/Sem1
Keywords keywordsPCI domain, TREX-2, gene expression, gene regulation; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.44
Radius of gyration Rg (electron density) rg_electron36.69
Forward intensity I(0) i0321342000.00
Molecular weight molecular_weight149190.0 kDa
Excluded volume excluded_volume188320 ų
Envelope volume envelope_volume246940 ų
Hydration-shell volume shell_volume54998 ų
Envelope diameter envelope_diameter134.4
Shell Rg shell_rg44.36
Envelope Rg envelope_rg35.69
Shape Rg shape_rg36.67
Total Rg total_rg37.26
Total atoms total_atoms10521
Residues n_residues1268
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 dmax124.0
Rg (real space) rg_real37.30
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real3.2130e+08
I(0) uncertainty (real space) i0_real_error5.3840e+06
Rg (reciprocal space) rg_reciprocal37.39
I(0) (reciprocal space) i0_reciprocal321400000.0000
Solution quality estimate total_estimate0.8904
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.2
Skewness Skewness skewness0.191
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha97410000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4trqA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily990
Domain ID domain_id4trqD00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily990

8. Citations (1)

9. Files and Curves (10)