2ecy

Solution structure of the Zinc finger, C3HC4 type (RING finger)" domain of TNF receptor-associated factor 3

Method: SOLUTION NMR Dmax: 70.1 Å Quality: REASONABLE

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

TNF receptor-associated factor 3

Homo sapiens

UniProt Q13114

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 43–101 Fragment:RING-type, residues 8-66 ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 7;296 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:1.10mM Protein; 20mM d-Tris-HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 50uM Zncl2+1mM IDA; 10% D2O, 90% H2O | 90% H2O/10% D2O Resolution not provided

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.

9 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRAF3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–66; UniProt 43–101

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 2ecy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ecy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ecy
Deposition date deposition_date2007-02-14
Structure title titleSolution structure of the Zinc finger, C3HC4 type (RING finger)" domain of TNF receptor-associated factor 3
Keywords keywords;Metal Binding Protein, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, APOPTOSIS ;; APOPTOSIS
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.67
Radius of gyration Rg (electron density) rg_electron15.90
Forward intensity I(0) i0350002000.00
Molecular weight molecular_weight144820.0 kDa
Excluded volume excluded_volume175990 ų
Envelope volume envelope_volume40744 ų
Hydration-shell volume shell_volume15069 ų
Envelope diameter envelope_diameter75.1
Shell Rg shell_rg29.50
Envelope Rg envelope_rg27.66
Shape Rg shape_rg16.02
Total Rg total_rg15.95
Total atoms total_atoms17640
Residues n_residues1320
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 dmax70.1
Rg (real space) rg_real16.46
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real3.5000e+08
I(0) uncertainty (real space) i0_real_error4.6700e+06
Rg (reciprocal space) rg_reciprocal16.37
I(0) (reciprocal space) i0_reciprocal350000000.0000
Solution quality estimate total_estimate0.6158
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.3
Skewness Skewness skewness1.107
Kurtosis Kurtosis kurtosis0.610
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha145600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.001; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.000; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)