4tqc

The co-complex structure of the translation initiation factor eIF4E with the inhibitor 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G

Method: X-RAY DIFFRACTION Dmax: 77.4 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 28–217 Fragment:UNP residues 28-217 M7G 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE × 1 34J (2S)-3-(4-amino-3-nitrophenyl)-2-{2-[(4P)-4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazin-1-yl}propanoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;290 K;PEG 4000 12-20%, 100mM MES pH 8.5, 10% IPN Resolution 1.80 Å R-free 0.194
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 28–217 Fragment:UNP residues 28-217 M7G 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;290 K;PEG 4000 12-20%, 100mM MES pH 8.5, 10% IPN Resolution 1.80 Å R-free 0.194

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 63 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 2–191; UniProt 28–217 Author chain B; PDBConstruct 2–191; UniProt 28–217

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 4tqc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4tqc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4tqc
Deposition date deposition_date2014-06-10
Structure title titleThe co-complex structure of the translation initiation factor eIF4E with the inhibitor 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G
Keywords keywordseIF4E, translation initiation inhibitor, allosteric, 4EGI1, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.55
Radius of gyration Rg (electron density) rg_electron22.30
Forward intensity I(0) i032653200.00
Molecular weight molecular_weight43016.0 kDa
Excluded volume excluded_volume53493 ų
Envelope volume envelope_volume64141 ų
Hydration-shell volume shell_volume24230 ų
Envelope diameter envelope_diameter79.5
Shell Rg shell_rg29.09
Envelope Rg envelope_rg22.49
Shape Rg shape_rg22.24
Total Rg total_rg23.34
Total atoms total_atoms5960
Residues n_residues355
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 dmax77.4
Rg (real space) rg_real23.56
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real3.2650e+07
I(0) uncertainty (real space) i0_real_error4.2610e+05
Rg (reciprocal space) rg_reciprocal23.56
I(0) (reciprocal space) i0_reciprocal32650000.0000
Solution quality estimate total_estimate0.8873
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.6
Skewness Skewness skewness0.374
Kurtosis Kurtosis kurtosis-0.375
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha6087000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4tqca_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.86 — eIF4e-like
Superfamily Superfamily superfamilyd.86.1 — eIF4e-like
Family Family familyd.86.1.1 — Translation initiation factor eIF4e
Domain ID domain_idd4tqcb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.86 — eIF4e-like
Superfamily Superfamily superfamilyd.86.1 — eIF4e-like
Family Family familyd.86.1.1 — Translation initiation factor eIF4e

CATH v4.4 (2 domains)

Domain ID domain_id4tqcA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology760 — RNA Cap, Translation Initiation Factor Eif4e
Homologous superfamily homologous superfamily10 — RNA Cap, Translation Initiation Factor Eif4e
Domain ID domain_id4tqcB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology760 — RNA Cap, Translation Initiation Factor Eif4e
Homologous superfamily homologous superfamily10 — RNA Cap, Translation Initiation Factor Eif4e

8. Citations (1)

9. Files and Curves (10)