1j2f

X-ray crystal structure of IRF-3 and its functional implications

Method: X-RAY DIFFRACTION Dmax: 85.2 Å Quality: EXCELLENT

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

Interferon regulatory factor 3

Homo sapiens

UniProt Q14653

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 175–427 Fragment:residues 170-427 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.2;277 K;magnesium formate, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.30 Å R-free 0.242
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 175–427 Fragment:residues 170-427 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.2;277 K;magnesium formate, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.30 Å R-free 0.242

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.

16 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IRF3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–258; UniProt 175–427 Author chain B; PDBConstruct 6–258; UniProt 175–427

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 1j2f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1j2f
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1j2f
Deposition date deposition_date2003-01-04
Structure title titleX-ray crystal structure of IRF-3 and its functional implications
Keywords keywordsTRANSCRIPTION FACTOR, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.67
Radius of gyration Rg (electron density) rg_electron25.59
Forward intensity I(0) i042077300.00
Molecular weight molecular_weight50556.0 kDa
Excluded volume excluded_volume63313 ų
Envelope volume envelope_volume79480 ų
Hydration-shell volume shell_volume26187 ų
Envelope diameter envelope_diameter89.9
Shell Rg shell_rg32.57
Envelope Rg envelope_rg25.32
Shape Rg shape_rg25.60
Total Rg total_rg26.38
Total atoms total_atoms3568
Residues n_residues457
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 dmax85.2
Rg (real space) rg_real26.66
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real4.2080e+07
I(0) uncertainty (real space) i0_real_error5.8140e+05
Rg (reciprocal space) rg_reciprocal26.67
I(0) (reciprocal space) i0_reciprocal42080000.0000
Solution quality estimate total_estimate0.9018
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.314
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11380000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1j2fa_
Class classb — All beta proteins
Fold Fold foldb.26 — SMAD/FHA domain
Superfamily Superfamily superfamilyb.26.1 — SMAD/FHA domain
Family Family familyb.26.1.3 — Interferon regulatory factor 3 (IRF3), transactivation domain
Domain ID domain_idd1j2fb_
Class classb — All beta proteins
Fold Fold foldb.26 — SMAD/FHA domain
Superfamily Superfamily superfamilyb.26.1 — SMAD/FHA domain
Family Family familyb.26.1.3 — Interferon regulatory factor 3 (IRF3), transactivation domain

CATH v4.4 (2 domains)

Domain ID domain_id1j2fA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily10
Domain ID domain_id1j2fB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)