4ncf

Crystal structure of eukaryotic translation initiation factor eIF5B (399-852) from Saccharomyces cerevisiae in complex with GDP

Method: X-RAY DIFFRACTION Dmax: 98.2 Å Quality: REASONABLE

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

Eukaryotic translation initiation factor 5B

Saccharomyces cerevisiae

UniProt P39730

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 399–852 Fragment:unp residues 399-852 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;283 K;8 % PEG 8000 0.37 M Li2SO4, VAPOR DIFFUSION, SITTING DROP, temperature 283K Resolution 3.02 Å R-free 0.281
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 399–852 Fragment:unp residues 399-852 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;283 K;8 % PEG 8000 0.37 M Li2SO4, VAPOR DIFFUSION, SITTING DROP, temperature 283K Resolution 3.02 Å R-free 0.281

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.

7 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF2P_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–457; UniProt 399–852 Author chain B; PDBConstruct 4–457; UniProt 399–852

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 4ncf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ncf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ncf
Deposition date deposition_date2013-10-24
Structure title titleCrystal structure of eukaryotic translation initiation factor eIF5B (399-852) from Saccharomyces cerevisiae in complex with GDP
Keywords keywordsTranslation initiation, GTPase, eIF5B/IF2, Subunit joining, Ribosome, TRANSLATION; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.53
Radius of gyration Rg (electron density) rg_electron30.64
Forward intensity I(0) i0142653000.00
Molecular weight molecular_weight95469.0 kDa
Excluded volume excluded_volume120020 ų
Envelope volume envelope_volume155780 ų
Hydration-shell volume shell_volume42209 ų
Envelope diameter envelope_diameter103.5
Shell Rg shell_rg37.93
Envelope Rg envelope_rg30.13
Shape Rg shape_rg30.68
Total Rg total_rg31.21
Total atoms total_atoms6699
Residues n_residues877
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 dmax98.2
Rg (real space) rg_real31.79
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real1.3970e+08
I(0) uncertainty (real space) i0_real_error1.6760e+06
Rg (reciprocal space) rg_reciprocal31.44
I(0) (reciprocal space) i0_reciprocal142700000.0000
Solution quality estimate total_estimate0.7128
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.2
Skewness Skewness skewness0.234
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha4.0730
Highest regularization parameter α highest_alpha44040000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 0.927; Sysdev: 0.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.707

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_id4ncfA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id4ncfA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id4ncfA03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10050 — Translation initiation factor IF- 2, domain 3
Domain ID domain_id4ncfB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id4ncfB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id4ncfB03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10050 — Translation initiation factor IF- 2, domain 3

8. Citations (1)

9. Files and Curves (10)