4k51

Crystal Structure of the PCI domain of eIF3a

Method: X-RAY DIFFRACTION Dmax: 181.0 Å Quality: REASONABLE

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

Eukaryotic translation initiation factor 3 subunit A

Saccharomyces cerevisiae

UniProt P38249

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 276–494 Fragment:PCI, UNP residues 276-494 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;PEG, buffer, salt, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.65 Å R-free 0.286
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 276–494 Fragment:PCI, UNP residues 276-494 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;PEG, buffer, salt, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.65 Å R-free 0.286

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.

12 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EIF3A_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–224; UniProt 276–494 Author chain B; PDBConstruct 6–224; UniProt 276–494

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 4k51

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4k51
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4k51
Deposition date deposition_date2013-04-12
Structure title titleCrystal Structure of the PCI domain of eIF3a
Keywords keywordseIF3, PCI domain, translation initiation, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier53.24
Radius of gyration Rg (electron density) rg_electron53.62
Forward intensity I(0) i023068100.00
Molecular weight molecular_weight42848.0 kDa
Excluded volume excluded_volume54762 ų
Envelope volume envelope_volume98703 ų
Hydration-shell volume shell_volume15443 ų
Envelope diameter envelope_diameter154.2
Shell Rg shell_rg60.19
Envelope Rg envelope_rg48.99
Shape Rg shape_rg53.64
Total Rg total_rg53.79
Total atoms total_atoms3032
Residues n_residues372
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 dmax181.0
Rg (real space) rg_real53.81
Rg uncertainty (real space) rg_real_error3.29
I(0) (real space) i0_real2.3070e+07
I(0) uncertainty (real space) i0_real_error5.7720e+05
Rg (reciprocal space) rg_reciprocal52.67
I(0) (reciprocal space) i0_reciprocal23030000.0000
Solution quality estimate total_estimate0.5392
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.107
Kurtosis Kurtosis kurtosis-1.669
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha706400.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.000; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.006; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4k51B00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily860

8. Citations (1)

9. Files and Curves (10)