9upc

Structure of human TREX-2

Method: ELECTRON MICROSCOPY Dmax: 101.0 Å Quality: EXCELLENT

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

Germinal-center associated nuclear protein

Homo sapiens

UniProt O60318

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 580–1000 Not recorded PCI domain-containing protein 2 × 1 (Q5JVF3) 26S proteasome complex subunit SEM1 × 1 (P60896) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;25 mM HEPES-KOH, pH 7.9, 150 mM NaCl, 1.5 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GANP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 43–463; UniProt 580–1000

PCI domain-containing protein 2

Homo sapiens

UniProt Q5JVF3

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–399 Fragment:3XFlag-PCID2 Germinal-center associated nuclear protein × 1 (O60318) 26S proteasome complex subunit SEM1 × 1 (P60896) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;25 mM HEPES-KOH, pH 7.9, 150 mM NaCl, 1.5 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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 PCID2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 28–426; UniProt 1–399

26S proteasome complex subunit SEM1

Homo sapiens

UniProt P60896

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–70 Not recorded Germinal-center associated nuclear protein × 1 (O60318) PCI domain-containing protein 2 × 1 (Q5JVF3) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9;25 mM HEPES-KOH, pH 7.9, 150 mM NaCl, 1.5 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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.

124 other PDB entries and 126 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEM1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–70; UniProt 1–70

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 9upc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9upc
Deposition date deposition_date2025-04-28
Structure title titleStructure of human TREX-2
Keywords keywordsmRNA nuclear export, TREX-2, UAP56, gene regulation; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.78
Radius of gyration Rg (electron density) rg_electron30.81
Forward intensity I(0) i0119730000.00
Molecular weight molecular_weight87434.0 kDa
Excluded volume excluded_volume109580 ų
Envelope volume envelope_volume135120 ų
Hydration-shell volume shell_volume36730 ų
Envelope diameter envelope_diameter100.8
Shell Rg shell_rg37.66
Envelope Rg envelope_rg30.78
Shape Rg shape_rg30.81
Total Rg total_rg31.39
Total atoms total_atoms6143
Residues n_residues759
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 dmax101.0
Rg (real space) rg_real31.71
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.1970e+08
I(0) uncertainty (real space) i0_real_error2.0050e+06
Rg (reciprocal space) rg_reciprocal31.74
I(0) (reciprocal space) i0_reciprocal119700000.0000
Solution quality estimate total_estimate0.9074
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.4
Skewness Skewness skewness0.188
Kurtosis Kurtosis kurtosis-0.655
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29130000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)