2ful

Crystal Structure of the C-terminal Domain of S. cerevisiae eIF5

Method: X-RAY DIFFRACTION Dmax: 153.9 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 241–405 Fragment:residues 236-412 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;277 K;2.8M (NH4)2SO4, 0.1M MES pH6.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.50 Å R-free 0.205
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 241–405 Fragment:residues 236-412 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;277 K;2.8M (NH4)2SO4, 0.1M MES pH6.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.50 Å R-free 0.205
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 241–405 Fragment:residues 236-412 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;277 K;2.8M (NH4)2SO4, 0.1M MES pH6.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.50 Å R-free 0.205
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 241–405 Fragment:residues 236-412 SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;277 K;2.8M (NH4)2SO4, 0.1M MES pH6.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.50 Å R-free 0.205
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 241–405 Fragment:residues 236-412 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;277 K;2.8M (NH4)2SO4, 0.1M MES pH6.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.50 Å R-free 0.205
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 241–405 Fragment:residues 236-412 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;277 K;2.8M (NH4)2SO4, 0.1M MES pH6.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.50 Å R-free 0.205

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 5 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 6–170; UniProt 241–405 Author chain B; PDBConstruct 6–170; UniProt 241–405 Author chain C; PDBConstruct 6–170; UniProt 241–405 Author chain D; PDBConstruct 6–170; UniProt 241–405 Author chain E; PDBConstruct 6–170; UniProt 241–405 Author chain F; PDBConstruct 6–170; UniProt 241–405

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 2ful

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ful
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ful
Deposition date deposition_date2006-01-27
Structure title titleCrystal Structure of the C-terminal Domain of S. cerevisiae eIF5
Keywords keywordsatypical HEAT motif, translation; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.38
Radius of gyration Rg (electron density) rg_electron41.66
Forward intensity I(0) i0185099000.00
Molecular weight molecular_weight112840.0 kDa
Excluded volume excluded_volume141940 ų
Envelope volume envelope_volume196970 ų
Hydration-shell volume shell_volume41669 ų
Envelope diameter envelope_diameter164.3
Shell Rg shell_rg43.47
Envelope Rg envelope_rg41.80
Shape Rg shape_rg41.66
Total Rg total_rg41.76
Total atoms total_atoms7929
Residues n_residues970
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 dmax153.9
Rg (real space) rg_real41.69
Rg uncertainty (real space) rg_real_error2.20
I(0) (real space) i0_real1.8510e+08
I(0) uncertainty (real space) i0_real_error3.8070e+06
Rg (reciprocal space) rg_reciprocal41.38
I(0) (reciprocal space) i0_reciprocal185000000.0000
Solution quality estimate total_estimate0.8152
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.5
Skewness Skewness skewness0.483
Kurtosis Kurtosis kurtosis-0.443
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15220000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.635; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.706; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id2fulA01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id2fulB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id2fulC01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id2fulD01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id2fulE01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id2fulF01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180

8. Citations (1)

9. Files and Curves (10)