6tvo

Human CRM1-RanGTP in complex with Leptomycin B

Method: X-RAY DIFFRACTION Dmax: 108.2 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–180 Mutation:Q69L Exportin-1 × 1 (O14980) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 LMB Leptomycin B, bound form × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277.15 K;0.02M sodium L-glutamate, 0.02M DL-alanine, 0.02M glycine, 0.02M DL-lysine HCl, 0.02 M DL-serine, 10%w/v PEG 8000, 20% v/v ethylene glycol, 0.1M bicine /Trizma base pH 8.5 Resolution 3.20 Å R-free 0.235

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 B; PDBConstruct 3–182; UniProt 1–180

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–1036 Mutation:V430A, L431A, V432A GTP-binding nuclear protein Ran × 1 (P62826) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 LMB Leptomycin B, bound form × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277.15 K;0.02M sodium L-glutamate, 0.02M DL-alanine, 0.02M glycine, 0.02M DL-lysine HCl, 0.02 M DL-serine, 10%w/v PEG 8000, 20% v/v ethylene glycol, 0.1M bicine /Trizma base pH 8.5 Resolution 3.20 Å R-free 0.235

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 2
Chains and sequence ranges Author chain A; PDBConstruct 15–1050; UniProt 1–1036

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 6tvo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6tvo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6tvo
Deposition date deposition_date2020-01-10
Structure title titleHuman CRM1-RanGTP in complex with Leptomycin B
Keywords keywordsCRM1, inhibitor, complex, Exportin 1, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.05
Radius of gyration Rg (electron density) rg_electron34.33
Forward intensity I(0) i0273046000.00
Molecular weight molecular_weight137610.0 kDa
Excluded volume excluded_volume174100 ų
Envelope volume envelope_volume223980 ų
Hydration-shell volume shell_volume52695 ų
Envelope diameter envelope_diameter109.4
Shell Rg shell_rg42.68
Envelope Rg envelope_rg33.69
Shape Rg shape_rg34.33
Total Rg total_rg34.96
Total atoms total_atoms9678
Residues n_residues1186
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 dmax108.2
Rg (real space) rg_real34.86
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real2.7300e+08
I(0) uncertainty (real space) i0_real_error4.4690e+06
Rg (reciprocal space) rg_reciprocal34.98
I(0) (reciprocal space) i0_reciprocal273100000.0000
Solution quality estimate total_estimate0.9090
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.7
Skewness Skewness skewness0.095
Kurtosis Kurtosis kurtosis-0.618
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha44560000.0000
Real-space data points n_real_points46
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: 0.989; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6tvoB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)