5sy5

Crystal Structure of the Heterodimeric NPAS1-ARNT Complex

Method: X-RAY DIFFRACTION Dmax: 189.2 Å Quality: REASONABLE

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

Aryl hydrocarbon receptor nuclear translocator

Mus musculus

UniProt P53762

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 82–464 Fragment:unp residues 82-464 Neuronal PAS domain-containing protein 1 × 1 (P97459) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate pH 7.0, 3% PEG3350 Resolution 3.20 Å R-free 0.247
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 82–464 Fragment:unp residues 82-464 Neuronal PAS domain-containing protein 1 × 1 (P97459) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate pH 7.0, 3% PEG3350 Resolution 3.20 Å R-free 0.247
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 82–464 Fragment:unp residues 82-464 Neuronal PAS domain-containing protein 1 × 1 (P97459) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate pH 7.0, 3% PEG3350 Resolution 3.20 Å R-free 0.247
4 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 82–464 Chain C; UniProt 82–464 Chain E; UniProt 82–464 Fragment:unp residues 82-464 Neuronal PAS domain-containing protein 1 × 3 (P97459) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate pH 7.0, 3% PEG3350 Resolution 3.20 Å R-free 0.247

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.

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

View Construct and Data Evidence
UniProt name ARNT_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–384; UniProt 82–464 Author chain C; PDBConstruct 2–384; UniProt 82–464 Author chain E; PDBConstruct 2–384; UniProt 82–464

Neuronal PAS domain-containing protein 1

Mus musculus

UniProt P97459

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 43–423 Fragment:unp reisdues 43-423 Aryl hydrocarbon receptor nuclear translocator × 1 (P53762) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate pH 7.0, 3% PEG3350 Resolution 3.20 Å R-free 0.247
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 43–423 Fragment:unp reisdues 43-423 Aryl hydrocarbon receptor nuclear translocator × 1 (P53762) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate pH 7.0, 3% PEG3350 Resolution 3.20 Å R-free 0.247
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 43–423 Fragment:unp reisdues 43-423 Aryl hydrocarbon receptor nuclear translocator × 1 (P53762) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate pH 7.0, 3% PEG3350 Resolution 3.20 Å R-free 0.247
4 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 43–423 Chain D; UniProt 43–423 Chain F; UniProt 43–423 Fragment:unp reisdues 43-423 Aryl hydrocarbon receptor nuclear translocator × 3 (P53762) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate pH 7.0, 3% PEG3350 Resolution 3.20 Å R-free 0.247

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name NPAS1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–383; UniProt 43–423 Author chain D; PDBConstruct 3–383; UniProt 43–423 Author chain F; PDBConstruct 3–383; UniProt 43–423

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 5sy5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5sy5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5sy5
Deposition date deposition_date2016-08-10
Structure title titleCrystal Structure of the Heterodimeric NPAS1-ARNT Complex
Keywords keywordsbHLH-PAS protein, transcription factor, heterodimeric complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier50.44
Radius of gyration Rg (electron density) rg_electron50.65
Forward intensity I(0) i0510852000.00
Molecular weight molecular_weight188850.0 kDa
Excluded volume excluded_volume237360 ų
Envelope volume envelope_volume346110 ų
Hydration-shell volume shell_volume62087 ų
Envelope diameter envelope_diameter197.1
Shell Rg shell_rg48.49
Envelope Rg envelope_rg49.72
Shape Rg shape_rg50.64
Total Rg total_rg50.60
Total atoms total_atoms13303
Residues n_residues1669
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 dmax189.2
Rg (real space) rg_real50.76
Rg uncertainty (real space) rg_real_error2.89
I(0) (real space) i0_real5.1090e+08
I(0) uncertainty (real space) i0_real_error9.2250e+06
Rg (reciprocal space) rg_reciprocal50.17
I(0) (reciprocal space) i0_reciprocal510500000.0000
Solution quality estimate total_estimate0.5806
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.9
Skewness Skewness skewness0.528
Kurtosis Kurtosis kurtosis-0.213
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22860000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.630; Stabil: 1.000; Sysdev: 0.003; Positv: 1.000; Valcen: 0.716; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)