5xln

Crystal structure of the TRS_UNE-T and 4EHP complex

Method: X-RAY DIFFRACTION Dmax: 65.2 Å Quality: REASONABLE

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

Eukaryotic translation initiation factor 4E type 2

Homo sapiens

UniProt O60573

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 45–234 Fragment:UNP residues 45-234 Threonine--tRNA ligase, cytoplasmic × 1 (P26639) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9.5;295 K;20% PEG 8000, 0.1 M CHES (pH 9.5) Resolution 1.90 Å R-free 0.196

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.

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

View Construct and Data Evidence
UniProt name IF4E2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–190; UniProt 45–234

Threonine--tRNA ligase, cytoplasmic

Homo sapiens

UniProt P26639

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 30–74 Fragment:UNP residues 30-74 Eukaryotic translation initiation factor 4E type 2 × 1 (O60573) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9.5;295 K;20% PEG 8000, 0.1 M CHES (pH 9.5) Resolution 1.90 Å R-free 0.196

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.

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYTC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–45; UniProt 30–74

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 5xln

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5xln
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5xln
Deposition date deposition_date2017-05-11
Structure title titleCrystal structure of the TRS_UNE-T and 4EHP complex
Keywords keywordsTRS, 4EHP, Complex, RNA BINDING PROTEIN-LIGASE complex; RNA BINDING PROTEIN/LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.74
Radius of gyration Rg (electron density) rg_electron16.44
Forward intensity I(0) i09121530.00
Molecular weight molecular_weight22338.0 kDa
Excluded volume excluded_volume28003 ų
Envelope volume envelope_volume32912 ų
Hydration-shell volume shell_volume16566 ų
Envelope diameter envelope_diameter59.3
Shell Rg shell_rg22.73
Envelope Rg envelope_rg17.07
Shape Rg shape_rg16.42
Total Rg total_rg17.56
Total atoms total_atoms1577
Residues n_residues191
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 dmax65.2
Rg (real space) rg_real17.62
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real9.1220e+06
I(0) uncertainty (real space) i0_real_error1.1790e+05
Rg (reciprocal space) rg_reciprocal17.64
I(0) (reciprocal space) i0_reciprocal9122000.0000
Solution quality estimate total_estimate0.7348
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.168
Kurtosis Kurtosis kurtosis-0.263
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2539000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.537; Stabil: 0.990; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5xlna_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.86 — eIF4e-like
Superfamily Superfamily superfamilyd.86.1 — eIF4e-like
Family Family familyd.86.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id5xlnA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology760 — RNA Cap, Translation Initiation Factor Eif4e
Homologous superfamily homologous superfamily10 — RNA Cap, Translation Initiation Factor Eif4e

8. Citations (1)

9. Files and Curves (10)