9f79

Crystal structure of the S. cerevisiae eIF2beta N-terminal tail bound to the C-terminal domain of eIF5

Method: X-RAY DIFFRACTION Dmax: 110.3 Å Quality: GOOD

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

Eukaryotic translation initiation factor 5

Saccharomyces cerevisiae

UniProt P38431

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 201–405 Chain B; UniProt 201–405 Not recorded Eukaryotic translation initiation factor 2 subunit beta × 2 (P09064) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;283 K;0.4 M (NH4)2SO4, 0.08 M Li2SO4 Resolution 2.00 Å R-free 0.228

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.

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

View Construct and Data Evidence
UniProt name IF5_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–210; UniProt 201–405 Author chain B; PDBConstruct 6–210; UniProt 201–405

Eukaryotic translation initiation factor 2 subunit beta

Saccharomyces cerevisiae

UniProt P09064

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 39–106 Not recorded Eukaryotic translation initiation factor 5 × 4 (P38431) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;283 K;0.4 M (NH4)2SO4, 0.08 M Li2SO4 Resolution 2.00 Å R-free 0.228

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.

23 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF2B_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 6–73; UniProt 39–106

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 9f79

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9f79
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9f79
Deposition date deposition_date2024-05-03
Structure title titleCrystal structure of the S. cerevisiae eIF2beta N-terminal tail bound to the C-terminal domain of eIF5
Keywords keywordsTranslation, Eukaryotic translation initiation factor, Complex, eIF5, W2 domain, eIF2 beta; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.31
Radius of gyration Rg (electron density) rg_electron28.57
Forward intensity I(0) i041397000.00
Molecular weight molecular_weight50495.0 kDa
Excluded volume excluded_volume63623 ų
Envelope volume envelope_volume90391 ų
Hydration-shell volume shell_volume27732 ų
Envelope diameter envelope_diameter114.9
Shell Rg shell_rg33.61
Envelope Rg envelope_rg29.66
Shape Rg shape_rg28.53
Total Rg total_rg29.28
Total atoms total_atoms3556
Residues n_residues447
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 dmax110.3
Rg (real space) rg_real29.39
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real4.1400e+07
I(0) uncertainty (real space) i0_real_error7.5280e+05
Rg (reciprocal space) rg_reciprocal29.36
I(0) (reciprocal space) i0_reciprocal41400000.0000
Solution quality estimate total_estimate0.8340
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.7
Skewness Skewness skewness0.421
Kurtosis Kurtosis kurtosis-0.085
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5096000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.683; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.853; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)