9upb

Structure of the human TREX-2 bound to UAP56

Method: ELECTRON MICROSCOPY Dmax: 102.4 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 × 4 PDB declaration: tetrameric(4) 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) Spliceosome RNA helicase DDX39B × 1 (Q13838) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 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 3.41 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 × 4 PDB declaration: tetrameric(4) 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) Spliceosome RNA helicase DDX39B × 1 (Q13838) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 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 3.41 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 × 4 PDB declaration: tetrameric(4) 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) Spliceosome RNA helicase DDX39B × 1 (Q13838) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 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 3.41 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

Spliceosome RNA helicase DDX39B

Homo sapiens

UniProt Q13838

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 1–428 Not recorded Germinal-center associated nuclear protein × 1 (O60318) PCI domain-containing protein 2 × 1 (Q5JVF3) 26S proteasome complex subunit SEM1 × 1 (P60896) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 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 3.41 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DX39B_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 28–455; UniProt 1–428

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 9upb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9upb
Deposition date deposition_date2025-04-28
Structure title titleStructure of the human TREX-2 bound to UAP56
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_guinier33.01
Radius of gyration Rg (electron density) rg_electron32.14
Forward intensity I(0) i0215456000.00
Molecular weight molecular_weight117830.0 kDa
Excluded volume excluded_volume147550 ų
Envelope volume envelope_volume182000 ų
Hydration-shell volume shell_volume46354 ų
Envelope diameter envelope_diameter108.1
Shell Rg shell_rg39.74
Envelope Rg envelope_rg32.02
Shape Rg shape_rg32.15
Total Rg total_rg32.71
Total atoms total_atoms8266
Residues n_residues1021
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 dmax102.4
Rg (real space) rg_real32.87
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real2.1550e+08
I(0) uncertainty (real space) i0_real_error2.8160e+06
Rg (reciprocal space) rg_reciprocal32.94
I(0) (reciprocal space) i0_reciprocal215500000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.6
Skewness Skewness skewness0.194
Kurtosis Kurtosis kurtosis-0.524
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76670000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.885

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)