8qm9

Potential drug binding sites for translation initiation factor eIF4E

Method: X-RAY DIFFRACTION Dmax: 83.5 Å Quality: GOOD

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

Eukaryotic translation initiation factor 4E

Homo sapiens

UniProt P06730

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 36–217 Chain B; UniProt 36–217 Not recorded EDO 1,2-ETHANEDIOL × 3 PEG DI(HYDROXYETHYL)ETHER × 4 DMS DIMETHYL SULFOXIDE × 2 W4K (2~{R})-2-[(1~{S})-1-[4-(2-fluorophenyl)-2-(2-hydroxyethylamino)phenyl]propoxy]propan-1-ol × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.002M DTT 38% PEG 400 0.1M pH=8 Tris/HCl Resolution 1.97 Å R-free 0.272

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.

44 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF4E_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 34–215; UniProt 36–217 Author chain B; PDBConstruct 34–215; UniProt 36–217

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 8qm9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8qm9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8qm9
Deposition date deposition_date2023-09-21
Structure title titlePotential drug binding sites for translation initiation factor eIF4E
Keywords keywordstranslation initiation factor, translation regulator, protein biosynthesis, RNA binding, TRANSLATION; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.80
Radius of gyration Rg (electron density) rg_electron23.97
Forward intensity I(0) i073643400.00
Molecular weight molecular_weight45019.0 kDa
Excluded volume excluded_volume43712 ų
Envelope volume envelope_volume74226 ų
Hydration-shell volume shell_volume25859 ų
Envelope diameter envelope_diameter87.7
Shell Rg shell_rg31.02
Envelope Rg envelope_rg24.20
Shape Rg shape_rg23.91
Total Rg total_rg24.70
Total atoms total_atoms3459
Residues n_residues404
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 dmax83.5
Rg (real space) rg_real24.80
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real7.3640e+07
I(0) uncertainty (real space) i0_real_error1.1660e+06
Rg (reciprocal space) rg_reciprocal24.80
I(0) (reciprocal space) i0_reciprocal73640000.0000
Solution quality estimate total_estimate0.8765
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.465
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11700000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)