8huj

Cryo-EM structure of the J-K-St region of EMCV IRES in complex with eIF4G-HEAT1 and eIF4A

Method: ELECTRON MICROSCOPY Dmax: 127.6 Å Quality: GOOD

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

Eukaryotic initiation factor 4A-I

Homo sapiens

UniProt P60842

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–RNA Heteromer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 2–406 Not recorded Eukaryotic translation initiation factor 4 gamma 1 × 1 (Q04637) IRES RNA (J-K-St) × 1 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.76 Å

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.

15 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF4A1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–428; UniProt 2–406

Eukaryotic translation initiation factor 4 gamma 1

Homo sapiens

UniProt Q04637

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–RNA Heteromer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain B; UniProt 746–992 Not recorded Eukaryotic initiation factor 4A-I × 1 (P60842) IRES RNA (J-K-St) × 1 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.76 Å

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.

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF4G1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 24–270; UniProt 746–992

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 8huj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8huj
Deposition date deposition_date2022-12-24
Structure title titleCryo-EM structure of the J-K-St region of EMCV IRES in complex with eIF4G-HEAT1 and eIF4A
Keywords keywordsTranslation initiation factors, Translation, RNA binding protein; TRANSLATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.95
Radius of gyration Rg (electron density) rg_electron36.65
Forward intensity I(0) i0250815000.00
Molecular weight molecular_weight103890.0 kDa
Excluded volume excluded_volume119970 ų
Envelope volume envelope_volume177150 ų
Hydration-shell volume shell_volume42733 ų
Envelope diameter envelope_diameter135.3
Shell Rg shell_rg40.53
Envelope Rg envelope_rg36.11
Shape Rg shape_rg36.57
Total Rg total_rg37.08
Total atoms total_atoms7142
Residues n_residues720
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 dmax127.6
Rg (real space) rg_real38.09
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real2.5080e+08
I(0) uncertainty (real space) i0_real_error4.0650e+06
Rg (reciprocal space) rg_reciprocal38.01
I(0) (reciprocal space) i0_reciprocal250800000.0000
Solution quality estimate total_estimate0.8842
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.5
Skewness Skewness skewness0.376
Kurtosis Kurtosis kurtosis-0.357
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9688000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.801

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)