6gd1

Structure of HuR RRM3

Method: X-RAY DIFFRACTION Dmax: 75.5 Å Quality: REASONABLE

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

Thioredoxin 1,ELAV-like protein 1

Homo sapiens

UniProt P0AA25

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–109 Chain B; UniProt 1–109 Not recorded NA SODIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;23% (w/v) PEG 2000 MME, 0.1 M potassium thiocyanate Resolution 2.01 Å R-free 0.244

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.

52 other PDB entries and 100 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THIO_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 10–118; UniProt 1–109 Author chain B; PDBConstruct 10–118; UniProt 1–109

Thioredoxin 1,ELAV-like protein 1

Homo sapiens

UniProt Q15717

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 243–326 Chain B; UniProt 243–326 Not recorded NA SODIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;23% (w/v) PEG 2000 MME, 0.1 M potassium thiocyanate Resolution 2.01 Å R-free 0.244

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.

10 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELAV1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 123–206; UniProt 243–326 Author chain B; PDBConstruct 123–206; UniProt 243–326

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 6gd1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6gd1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6gd1
Deposition date deposition_date2018-04-21
Structure title titleStructure of HuR RRM3
Keywords keywordsRNA binding protein; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.74
Radius of gyration Rg (electron density) rg_electron21.78
Forward intensity I(0) i025821300.00
Molecular weight molecular_weight40928.0 kDa
Excluded volume excluded_volume52013 ų
Envelope volume envelope_volume61704 ų
Hydration-shell volume shell_volume23927 ų
Envelope diameter envelope_diameter78.2
Shell Rg shell_rg28.33
Envelope Rg envelope_rg21.74
Shape Rg shape_rg21.79
Total Rg total_rg22.58
Total atoms total_atoms2879
Residues n_residues377
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 dmax75.5
Rg (real space) rg_real22.73
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real2.5820e+07
I(0) uncertainty (real space) i0_real_error3.6180e+05
Rg (reciprocal space) rg_reciprocal22.73
I(0) (reciprocal space) i0_reciprocal25820000.0000
Solution quality estimate total_estimate0.6727
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.3
Skewness Skewness skewness0.392
Kurtosis Kurtosis kurtosis-0.156
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6297000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 1.000; Sysdev: 0.130; Positv: 1.000; Valcen: 1.000; Smooth: 0.959

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_id6gd1A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id6gd1B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin

8. Citations (1)

9. Files and Curves (10)