9ogn

Crystal Structure of KPT396 in complex with CRM1-Ran-RanBP1

Method: X-RAY DIFFRACTION Dmax: 109.0 Å Quality: EXCELLENT

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

GTP-binding nuclear protein Ran

Homo sapiens

UniProt P62826

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 1–216 Not recorded Ran-specific GTPase-activating protein 1 × 1 (P41920) Exportin-1 × 1 (P30822) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 3 CL CHLORIDE ION × 3 A1CBD 3-(3-{3-[(but-2-yn-1-yl)oxy]-5-(trifluoromethyl)phenyl}-1H-1,2,4-triazol-1-yl)-N-(piperidin-1-yl)propanamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;17% PEG3350, 100 mM Bis-Tris (pH 6.6) and 200 mM ammonium nitrate Resolution 2.41 Å R-free 0.224

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.

137 other PDB entries and 203 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–237; UniProt 1–216

Ran-specific GTPase-activating protein 1

Saccharomyces cerevisiae

UniProt P41920

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 62–201 Not recorded GTP-binding nuclear protein Ran × 1 (P62826) Exportin-1 × 1 (P30822) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 3 CL CHLORIDE ION × 3 A1CBD 3-(3-{3-[(but-2-yn-1-yl)oxy]-5-(trifluoromethyl)phenyl}-1H-1,2,4-triazol-1-yl)-N-(piperidin-1-yl)propanamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;17% PEG3350, 100 mM Bis-Tris (pH 6.6) and 200 mM ammonium nitrate Resolution 2.41 Å R-free 0.224

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.

65 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YRB1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–143; UniProt 62–201

Exportin-1

Saccharomyces cerevisiae

UniProt P30822

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 1–1058 Mutation:T539C, Y1022C GTP-binding nuclear protein Ran × 1 (P62826) Ran-specific GTPase-activating protein 1 × 1 (P41920) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 3 CL CHLORIDE ION × 3 A1CBD 3-(3-{3-[(but-2-yn-1-yl)oxy]-5-(trifluoromethyl)phenyl}-1H-1,2,4-triazol-1-yl)-N-(piperidin-1-yl)propanamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;17% PEG3350, 100 mM Bis-Tris (pH 6.6) and 200 mM ammonium nitrate Resolution 2.41 Å R-free 0.224

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.

69 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XPO1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–1024; UniProt 1–1058

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 9ogn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ogn
Deposition date deposition_date2025-05-01
Structure title titleCrystal Structure of KPT396 in complex with CRM1-Ran-RanBP1
Keywords keywordsExportin, SINE, Export, XPO1, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.05
Radius of gyration Rg (electron density) rg_electron35.20
Forward intensity I(0) i0342329000.00
Molecular weight molecular_weight154890.0 kDa
Excluded volume excluded_volume195990 ų
Envelope volume envelope_volume252610 ų
Hydration-shell volume shell_volume57596 ų
Envelope diameter envelope_diameter109.0
Shell Rg shell_rg43.67
Envelope Rg envelope_rg34.49
Shape Rg shape_rg35.19
Total Rg total_rg35.83
Total atoms total_atoms21849
Residues n_residues1338
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 dmax109.0
Rg (real space) rg_real35.80
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real3.4230e+08
I(0) uncertainty (real space) i0_real_error6.3860e+06
Rg (reciprocal space) rg_reciprocal35.96
I(0) (reciprocal space) i0_reciprocal342400000.0000
Solution quality estimate total_estimate0.9064
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.1
Skewness Skewness skewness0.040
Kurtosis Kurtosis kurtosis-0.612
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha52100000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)