6b4f

Crystal structure of human Gle1 CTD-Nup42 GBM complex

Method: X-RAY DIFFRACTION Dmax: 98.4 Å Quality: REASONABLE

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

Nucleoporin GLE1

Homo sapiens

UniProt Q53GS7

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 383–698 Not recorded Nucleoporin like 2 × 1 (Q3B7J4) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.2 M sodium potassium phosphate pH 7.6, 26 % (w/v) PEG 3350 Resolution 2.81 Å R-free 0.274
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 383–698 Not recorded Nucleoporin like 2 × 1 (Q3B7J4) PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.2 M sodium potassium phosphate pH 7.6, 26 % (w/v) PEG 3350 Resolution 2.81 Å R-free 0.274

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLE1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–317; UniProt 383–698 Author chain B; PDBConstruct 2–317; UniProt 383–698

Nucleoporin like 2

Homo sapiens

UniProt Q3B7J4

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 C; UniProt 381–423 Not recorded Nucleoporin GLE1 × 1 (Q53GS7) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.2 M sodium potassium phosphate pH 7.6, 26 % (w/v) PEG 3350 Resolution 2.81 Å R-free 0.274
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 381–423 Not recorded Nucleoporin GLE1 × 1 (Q53GS7) PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.2 M sodium potassium phosphate pH 7.6, 26 % (w/v) PEG 3350 Resolution 2.81 Å R-free 0.274

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q3B7J4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 8–50; UniProt 381–423 Author chain D; PDBConstruct 8–50; UniProt 381–423

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 6b4f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6b4f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6b4f
Deposition date deposition_date2017-09-26
Structure title titleCrystal structure of human Gle1 CTD-Nup42 GBM complex
Keywords keywordsComplex, Nuclear Pore Complex, mRNA export, DEAD-box helicase, 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_guinier29.80
Radius of gyration Rg (electron density) rg_electron28.79
Forward intensity I(0) i0100996000.00
Molecular weight molecular_weight82479.0 kDa
Excluded volume excluded_volume104670 ų
Envelope volume envelope_volume132540 ų
Hydration-shell volume shell_volume37680 ų
Envelope diameter envelope_diameter101.3
Shell Rg shell_rg36.58
Envelope Rg envelope_rg29.08
Shape Rg shape_rg28.73
Total Rg total_rg29.77
Total atoms total_atoms11682
Residues n_residues718
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 dmax98.4
Rg (real space) rg_real29.76
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.0100e+08
I(0) uncertainty (real space) i0_real_error1.4890e+06
Rg (reciprocal space) rg_reciprocal29.78
I(0) (reciprocal space) i0_reciprocal101000000.0000
Solution quality estimate total_estimate0.6871
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.4
Skewness Skewness skewness0.320
Kurtosis Kurtosis kurtosis-0.343
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24850000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 0.135; Positv: 1.000; Valcen: 0.999; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)