9i9f

Crystal structure of apoform human eIF4A1 C-terminal domain

Method: X-RAY DIFFRACTION Dmax: 84.3 Å Quality: EXCELLENT

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 239–406 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;18.5% (w/v) PEG 8000, 0.2M sodium acetate trihydrate, 0.1M MES, pH 6.0 Resolution 2.73 Å R-free 0.294
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 239–406 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;18.5% (w/v) PEG 8000, 0.2M sodium acetate trihydrate, 0.1M MES, pH 6.0 Resolution 2.73 Å R-free 0.294
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 239–406 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;18.5% (w/v) PEG 8000, 0.2M sodium acetate trihydrate, 0.1M MES, pH 6.0 Resolution 2.73 Å R-free 0.294

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 20 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 3–170; UniProt 239–406 Author chain B; PDBConstruct 3–170; UniProt 239–406 Author chain C; PDBConstruct 3–170; UniProt 239–406

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 9i9f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9i9f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9i9f
Deposition date deposition_date2025-02-06
最后修订 last_revision2026-02-18
Structure title titleCrystal structure of apoform human eIF4A1 C-terminal domain
Keywords keywordsINITIATION FACTOR, DEAD-BOX, HELICASE, ATPASE, TRANSLATION; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.89
Radius of gyration Rg (electron density) rg_electron26.82
Forward intensity I(0) i047088100.00
Molecular weight molecular_weight53051.0 kDa
Excluded volume excluded_volume66398 ų
Envelope volume envelope_volume86189 ų
Hydration-shell volume shell_volume27600 ų
Envelope diameter envelope_diameter87.2
Shell Rg shell_rg33.19
Envelope Rg envelope_rg26.54
Shape Rg shape_rg26.81
Total Rg total_rg27.59
Total atoms total_atoms3732
Residues n_residues486
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 dmax84.3
Rg (real space) rg_real27.80
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real4.7090e+07
I(0) uncertainty (real space) i0_real_error6.7940e+05
Rg (reciprocal space) rg_reciprocal27.83
I(0) (reciprocal space) i0_reciprocal47090000.0000
Solution quality estimate total_estimate0.9112
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.6
Skewness Skewness skewness0.138
Kurtosis Kurtosis kurtosis-0.736
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14450000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.969; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)