9oge

Cryo-EM structure of human exportin-1 conjugated with KPT-127 and bound to human ASB8-ELOB/C

Method: ELECTRON MICROSCOPY Dmax: 157.6 Å Quality: GOOD

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

Exportin-1

Homo sapiens

UniProt O14980

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 1–1071 Not recorded Ankyrin repeat and SOCS box protein 8 × 1 (Q9H765) Elongin-C × 1 (Q15369) Elongin-B × 1 (Q15370) A1CBC propan-2-yl 3-[3-(3-chlorophenyl)-1H-1,2,4-triazol-1-yl]propanoate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM HEPES pH 7.4, 110 mM KOAc, 2 mM Mg(OAc)2, 2 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.28 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XPO1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–1073; UniProt 1–1071

Ankyrin repeat and SOCS box protein 8

Homo sapiens

UniProt Q9H765

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 17–288 Fragment:residues 17-288 Exportin-1 × 1 (O14980) Elongin-C × 1 (Q15369) Elongin-B × 1 (Q15370) A1CBC propan-2-yl 3-[3-(3-chlorophenyl)-1H-1,2,4-triazol-1-yl]propanoate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM HEPES pH 7.4, 110 mM KOAc, 2 mM Mg(OAc)2, 2 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.28 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASB8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–274; UniProt 17–288

Elongin-C

Homo sapiens

UniProt Q15369

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 E; UniProt 17–112 Fragment:residues 17-112 Exportin-1 × 1 (O14980) Ankyrin repeat and SOCS box protein 8 × 1 (Q9H765) Elongin-B × 1 (Q15370) A1CBC propan-2-yl 3-[3-(3-chlorophenyl)-1H-1,2,4-triazol-1-yl]propanoate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM HEPES pH 7.4, 110 mM KOAc, 2 mM Mg(OAc)2, 2 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.28 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.

220 other PDB entries and 467 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 2–97; UniProt 17–112

Elongin-B

Homo sapiens

UniProt Q15370

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 F; UniProt 1–118 Not recorded Exportin-1 × 1 (O14980) Ankyrin repeat and SOCS box protein 8 × 1 (Q9H765) Elongin-C × 1 (Q15369) A1CBC propan-2-yl 3-[3-(3-chlorophenyl)-1H-1,2,4-triazol-1-yl]propanoate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM HEPES pH 7.4, 110 mM KOAc, 2 mM Mg(OAc)2, 2 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.28 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.

228 other PDB entries and 478 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–118; UniProt 1–118

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 9oge

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9oge
Deposition date deposition_date2025-04-30
Structure title titleCryo-EM structure of human exportin-1 conjugated with KPT-127 and bound to human ASB8-ELOB/C
Keywords keywordsnuclear export, inhibitor, protein degradation, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.06
Radius of gyration Rg (electron density) rg_electron44.59
Forward intensity I(0) i0245863000.00
Molecular weight molecular_weight131720.0 kDa
Excluded volume excluded_volume166360 ų
Envelope volume envelope_volume227360 ų
Hydration-shell volume shell_volume47188 ų
Envelope diameter envelope_diameter165.9
Shell Rg shell_rg43.78
Envelope Rg envelope_rg43.85
Shape Rg shape_rg44.58
Total Rg total_rg44.59
Total atoms total_atoms18551
Residues n_residues1154
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 dmax157.6
Rg (real space) rg_real44.47
Rg uncertainty (real space) rg_real_error2.09
I(0) (real space) i0_real2.4590e+08
I(0) uncertainty (real space) i0_real_error4.8560e+06
Rg (reciprocal space) rg_reciprocal44.06
I(0) (reciprocal space) i0_reciprocal245700000.0000
Solution quality estimate total_estimate0.8249
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.5
Skewness Skewness skewness0.549
Kurtosis Kurtosis kurtosis-0.094
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18800000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.754; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.779; Smooth: 0.679

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)