5eir

Co-crystal structure of eIF4E with nucleotide mimetic inhibitor.

Method: X-RAY DIFFRACTION Dmax: 63.9 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–217 Not recorded Eukaryotic translation initiation factor 4 gamma 1 × 1 5O8 ~{N}-[[(2~{R},3~{S},4~{R},5~{R})-5-[2-azanyl-6-oxidanylidene-7-(phenylmethyl)-1~{H}-purin-7-ium-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-1,1,1-tris(fluoranyl)methanesulfonamide × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;21-31% PEG 8000, 1???3% (NH4)2SO4, 100 mM HEPES, pH 7.5, 1 round of seeding. Crystals replaced in to above conditions without (NH4)2SO4 prior to freezing. Resolution 2.69 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 1–217; 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 5eir

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5eir
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5eir
Deposition date deposition_date2015-10-30
Structure title titleCo-crystal structure of eIF4E with nucleotide mimetic inhibitor.
Keywords keywordsComplex, inhibitor, translation, eIF4E; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.17
Radius of gyration Rg (electron density) rg_electron16.99
Forward intensity I(0) i010817300.00
Molecular weight molecular_weight24118.0 kDa
Excluded volume excluded_volume30098 ų
Envelope volume envelope_volume35256 ų
Hydration-shell volume shell_volume17300 ų
Envelope diameter envelope_diameter66.0
Shell Rg shell_rg23.36
Envelope Rg envelope_rg17.65
Shape Rg shape_rg16.95
Total Rg total_rg18.16
Total atoms total_atoms1702
Residues n_residues199
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 dmax63.9
Rg (real space) rg_real18.09
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.0820e+07
I(0) uncertainty (real space) i0_real_error1.4330e+05
Rg (reciprocal space) rg_reciprocal18.10
I(0) (reciprocal space) i0_reciprocal10820000.0000
Solution quality estimate total_estimate0.7614
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.312
Kurtosis Kurtosis kurtosis0.008
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3420000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.633; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

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_id5eirA00
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)