4iul

MIF4G domain of DAP5

Method: X-RAY DIFFRACTION Dmax: 93.6 Å Quality: GOOD

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

Eukaryotic translation initiation factor 4 gamma 2

Homo sapiens

UniProt P78344

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 61–323 Fragment:MIF4G domain, UNP residues 61-323 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;0.1 M HEPES pH 7.5, 0.2 M ammonium sulfate and 18 20% (w/v) polyethylene glycol 5000 monomethyl ether, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.30 Å R-free 0.256
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 61–323 Fragment:MIF4G domain, UNP residues 61-323 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;0.1 M HEPES pH 7.5, 0.2 M ammonium sulfate and 18 20% (w/v) polyethylene glycol 5000 monomethyl ether, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.30 Å R-free 0.256
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 61–323 Chain B; UniProt 61–323 Fragment:MIF4G domain, UNP residues 61-323 SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;0.1 M HEPES pH 7.5, 0.2 M ammonium sulfate and 18 20% (w/v) polyethylene glycol 5000 monomethyl ether, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.30 Å R-free 0.256

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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF4G2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–268; UniProt 61–323 Author chain B; PDBConstruct 6–268; UniProt 61–323

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 4iul

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4iul
Deposition date deposition_date2013-01-21
Structure title titleMIF4G domain of DAP5
Keywords keywordsHEAT repeats, protein-protein interaction, eIF4A, TRANSLATION; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.94
Radius of gyration Rg (electron density) rg_electron27.18
Forward intensity I(0) i049036400.00
Molecular weight molecular_weight54843.0 kDa
Excluded volume excluded_volume69054 ų
Envelope volume envelope_volume88998 ų
Hydration-shell volume shell_volume27753 ų
Envelope diameter envelope_diameter96.7
Shell Rg shell_rg33.81
Envelope Rg envelope_rg27.34
Shape Rg shape_rg27.16
Total Rg total_rg27.94
Total atoms total_atoms3835
Residues n_residues469
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 dmax93.6
Rg (real space) rg_real27.96
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real4.9040e+07
I(0) uncertainty (real space) i0_real_error7.0020e+05
Rg (reciprocal space) rg_reciprocal27.96
I(0) (reciprocal space) i0_reciprocal49040000.0000
Solution quality estimate total_estimate0.8920
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.2
Skewness Skewness skewness0.327
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9307000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4iulA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id4iulB00
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)