9dlr

Cryo-EM structure of the human TREX-2.1 complex (LENG8/PCID2/DSS1) bound to the N-terminal motif of DDX39B(UAP56)

Method: ELECTRON MICROSCOPY Dmax: 103.5 Å Quality: GOOD

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

Leukocyte receptor cluster member 8

Homo sapiens

UniProt Q96PV6

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 490–800 Not recorded PCI domain-containing protein 2 × 1 (Q5JVF3) 26S proteasome complex subunit SEM1 × 1 (P60896) Spliceosome RNA helicase DDX39B × 1 (Q13838) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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 LENG8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–316; UniProt 490–800

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 Not recorded Leukocyte receptor cluster member 8 × 1 (Q96PV6) 26S proteasome complex subunit SEM1 × 1 (P60896) Spliceosome RNA helicase DDX39B × 1 (Q13838) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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 1–399; 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 Leukocyte receptor cluster member 8 × 1 (Q96PV6) PCI domain-containing protein 2 × 1 (Q5JVF3) Spliceosome RNA helicase DDX39B × 1 (Q13838) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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 Leukocyte receptor cluster member 8 × 1 (Q96PV6) PCI domain-containing protein 2 × 1 (Q5JVF3) 26S proteasome complex subunit SEM1 × 1 (P60896) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.08 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 1–428; 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 9dlr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dlr
Deposition date deposition_date2024-09-11
Structure title titleCryo-EM structure of the human TREX-2.1 complex (LENG8/PCID2/DSS1) bound to the N-terminal motif of DDX39B(UAP56)
Keywords keywordsmRNA nuclear export, TREX, TREX-2, LENG8, UAP56, DDX39B, RNA BINDING PROTEIN, RNA BINDING PROTEIN-Hydrolase complex; RNA BINDING PROTEIN/Hydrolase
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.60
Radius of gyration Rg (electron density) rg_electron30.74
Forward intensity I(0) i092358300.00
Molecular weight molecular_weight77850.0 kDa
Excluded volume excluded_volume98120 ų
Envelope volume envelope_volume123150 ų
Hydration-shell volume shell_volume34249 ų
Envelope diameter envelope_diameter106.6
Shell Rg shell_rg36.76
Envelope Rg envelope_rg30.60
Shape Rg shape_rg30.73
Total Rg total_rg31.33
Total atoms total_atoms5480
Residues n_residues676
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 dmax103.5
Rg (real space) rg_real31.60
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real9.2360e+07
I(0) uncertainty (real space) i0_real_error1.4430e+06
Rg (reciprocal space) rg_reciprocal31.60
I(0) (reciprocal space) i0_reciprocal92360000.0000
Solution quality estimate total_estimate0.8980
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.2
Skewness Skewness skewness0.276
Kurtosis Kurtosis kurtosis-0.513
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16980000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)