8t5q

SARS-CoV-2 ORF3a peptide in complex with TRAF2 TRAF domain

Method: X-RAY DIFFRACTION Dmax: 116.1 Å Quality: GOOD

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

TNF receptor-associated factor 2

Homo sapiens

UniProt Q12933

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 315–501 Chain B; UniProt 315–501 Chain C; UniProt 315–501 Fragment:TRAF domain (UNP residues 315-501) ORF3a protein × 2 (P0DTC3) PG4 TETRAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;277.15 K;0.1 M sodium citrate, pH 5.0, 20% w/v PEG8000 Resolution 1.90 Å R-free 0.240
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 315–501 Chain E; UniProt 315–501 Chain F; UniProt 315–501 Fragment:TRAF domain (UNP residues 315-501) ORF3a protein × 1 (P0DTC3) PG4 TETRAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;277.15 K;0.1 M sodium citrate, pH 5.0, 20% w/v PEG8000 Resolution 1.90 Å R-free 0.240

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.

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

View Construct and Data Evidence
UniProt name TRAF2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–188; UniProt 315–501 Author chain B; PDBConstruct 2–188; UniProt 315–501 Author chain C; PDBConstruct 2–188; UniProt 315–501 Author chain D; PDBConstruct 2–188; UniProt 315–501 Author chain E; PDBConstruct 2–188; UniProt 315–501 Author chain F; PDBConstruct 2–188; UniProt 315–501

ORF3a protein

OrganismNot specified

UniProt P0DTC3

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 36–40 Chain H; UniProt 36–40 Fragment:UNP residues 36-40 TNF receptor-associated factor 2 × 3 (Q12933) PG4 TETRAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;277.15 K;0.1 M sodium citrate, pH 5.0, 20% w/v PEG8000 Resolution 1.90 Å R-free 0.240
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain I; UniProt 36–40 Fragment:UNP residues 36-40 TNF receptor-associated factor 2 × 3 (Q12933) PG4 TETRAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;277.15 K;0.1 M sodium citrate, pH 5.0, 20% w/v PEG8000 Resolution 1.90 Å R-free 0.240

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.

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP3A_SARS2
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–5; UniProt 36–40 Author chain H; PDBConstruct 1–5; UniProt 36–40 Author chain I; PDBConstruct 1–5; UniProt 36–40

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 8t5q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t5q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t5q
Deposition date deposition_date2023-06-14
Structure title titleSARS-CoV-2 ORF3a peptide in complex with TRAF2 TRAF domain
Keywords keywordssignaling protein-viral protein complex; SIGNALING PROTEIN/VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.80
Radius of gyration Rg (electron density) rg_electron37.41
Forward intensity I(0) i0201250000.00
Molecular weight molecular_weight116620.0 kDa
Excluded volume excluded_volume146790 ų
Envelope volume envelope_volume194540 ų
Hydration-shell volume shell_volume45442 ų
Envelope diameter envelope_diameter123.0
Shell Rg shell_rg41.34
Envelope Rg envelope_rg36.96
Shape Rg shape_rg37.39
Total Rg total_rg37.73
Total atoms total_atoms8189
Residues n_residues1023
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 dmax116.1
Rg (real space) rg_real37.97
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real2.0120e+08
I(0) uncertainty (real space) i0_real_error3.3510e+06
Rg (reciprocal space) rg_reciprocal37.87
I(0) (reciprocal space) i0_reciprocal201200000.0000
Solution quality estimate total_estimate0.8308
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.7
Skewness Skewness skewness0.441
Kurtosis Kurtosis kurtosis-0.390
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28690000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.025

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)