4dum

Co-crystal structure of eIF4E with inhibitor

Method: X-RAY DIFFRACTION Dmax: 73.2 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 1–217 Not recorded HLI (4-{7-[2-(4-chlorophenoxy)ethyl]-2-(methylamino)-6-oxo-6,7-dihydro-1H-purin-8-yl}phenyl)phosphonic acid × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;The purified protein which contained 100 uM m7-GTP was then concentrated to about 7 mg/mL in 20 mM Hepes, pH7.6, 100 mM KCl, 1mM DTT, 0.1 mM EDTA for crystallization. The m7-GTP-bound eIF4e protein was crystallized with 1:1 ratio of protein solution to reservoir solution of 17-20% PEG-3350 and 0.1-0.4M Na formate, VAPOR DIFFUSION, SITTING DROP, temperature 289K Resolution 2.95 Å R-free 0.271

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 24–240; UniProt 1–217

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 4dum

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4dum
Deposition date deposition_date2012-02-22
Structure title titleCo-crystal structure of eIF4E with inhibitor
Keywords keywordsCAP-binding protein, translation initiation factor, m7GTP, TRANSLATION; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.24
Radius of gyration Rg (electron density) rg_electron17.10
Forward intensity I(0) i09443070.00
Molecular weight molecular_weight22494.0 kDa
Excluded volume excluded_volume28088 ų
Envelope volume envelope_volume32958 ų
Hydration-shell volume shell_volume16452 ų
Envelope diameter envelope_diameter74.0
Shell Rg shell_rg23.10
Envelope Rg envelope_rg18.02
Shape Rg shape_rg17.06
Total Rg total_rg18.21
Total atoms total_atoms1587
Residues n_residues187
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 dmax73.2
Rg (real space) rg_real18.25
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real9.4430e+06
I(0) uncertainty (real space) i0_real_error1.4490e+05
Rg (reciprocal space) rg_reciprocal18.25
I(0) (reciprocal space) i0_reciprocal9443000.0000
Solution quality estimate total_estimate0.7616
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.513
Kurtosis Kurtosis kurtosis0.496
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2688000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.350; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.850; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4duma_
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 (1 domains)

Domain ID domain_id4dumA00
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)