1t2k

Structure Of The DNA Binding Domains Of IRF3, ATF-2 and Jun Bound To DNA

Method: X-RAY DIFFRACTION Dmax: 113.5 Å Quality: GOOD

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–112 Chain B; UniProt 1–112 Fragment:N-terminal DNA binding domain 31-MER × 1 31-MER × 1 Transcription factor AP-1 × 1 (P05412) Cyclic-AMP-dependent transcription factor ATF-2 × 1 (P15336) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;100 mM NaCacodylate, pH 6.5, 12.5% (w/v) PEG 6000, 400 mM NH4OAc, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 3.00 Å R-free 0.296

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 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IRF3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–112; UniProt 1–112 Author chain B; PDBConstruct 1–112; UniProt 1–112

Transcription factor AP-1

Homo sapiens

UniProt P05412

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 254–314 Fragment:bZip domain Mutation:C269S 31-MER × 1 31-MER × 1 Interferon regulatory factor 3 × 2 (Q14653) Cyclic-AMP-dependent transcription factor ATF-2 × 1 (P15336) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;100 mM NaCacodylate, pH 6.5, 12.5% (w/v) PEG 6000, 400 mM NH4OAc, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 3.00 Å R-free 0.296

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name JUN_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–62; UniProt 254–314

Cyclic-AMP-dependent transcription factor ATF-2

Homo sapiens

UniProt P15336

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain D; UniProt 336–396 Fragment:bZip domain Mutation:C351S 31-MER × 1 31-MER × 1 Interferon regulatory factor 3 × 2 (Q14653) Transcription factor AP-1 × 1 (P05412) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;100 mM NaCacodylate, pH 6.5, 12.5% (w/v) PEG 6000, 400 mM NH4OAc, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 3.00 Å R-free 0.296

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 ATF2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain D; PDBConstruct 1–61; UniProt 336–396

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 1t2k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1t2k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1t2k
Deposition date deposition_date2004-04-21
Structure title titleStructure Of The DNA Binding Domains Of IRF3, ATF-2 and Jun Bound To DNA
Keywords keywordsPROTEIN DNA COMPLEX, transcription, Transcription-DNA COMPLEX; Transcription/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.19
Radius of gyration Rg (electron density) rg_electron31.56
Forward intensity I(0) i081212500.00
Molecular weight molecular_weight58139.0 kDa
Excluded volume excluded_volume67291 ų
Envelope volume envelope_volume99130 ų
Hydration-shell volume shell_volume28674 ų
Envelope diameter envelope_diameter119.8
Shell Rg shell_rg34.87
Envelope Rg envelope_rg32.19
Shape Rg shape_rg31.52
Total Rg total_rg31.91
Total atoms total_atoms4026
Residues n_residues403
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 dmax113.5
Rg (real space) rg_real31.54
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real8.1210e+07
I(0) uncertainty (real space) i0_real_error1.2970e+06
Rg (reciprocal space) rg_reciprocal31.40
I(0) (reciprocal space) i0_reciprocal81200000.0000
Solution quality estimate total_estimate0.8049
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.568
Kurtosis Kurtosis kurtosis-0.202
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6770000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.677; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.484; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd1t2ka_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.23 — Interferon regulatory factor
Domain ID domain_idd1t2kb_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.23 — Interferon regulatory factor
Domain ID domain_idd1t2kc1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain
Domain ID domain_idd1t2kc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1t2kd_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain

CATH v4.4 (4 domains)

Domain ID domain_id1t2kA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Domain ID domain_id1t2kB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Domain ID domain_id1t2kC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170
Domain ID domain_id1t2kD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170

8. Citations (1)

9. Files and Curves (10)