8vhg

Structure of the BMAL1/HIF2A heterodimer in Complex with DNA

Method: ELECTRON MICROSCOPY Dmax: 119.2 Å Quality: GOOD

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

Endothelial PAS domain-containing protein 1

Mus musculus

UniProt P97481

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 × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 3–361 Not recorded Basic helix-loop-helix ARNT-like protein 1 × 1 (Q9WTL8) Reverse strand DNA containing HRE motif × 1 Forward strand DNA containing HRE motif × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 Å

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.

12 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EPAS1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–380; UniProt 3–361

Basic helix-loop-helix ARNT-like protein 1

Mus musculus

UniProt Q9WTL8

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 × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 75–494 Not recorded Endothelial PAS domain-containing protein 1 × 1 (P97481) Reverse strand DNA containing HRE motif × 1 Forward strand DNA containing HRE motif × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BMAL1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–421; UniProt 75–494

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 8vhg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vhg
Deposition date deposition_date2024-01-01
Structure title titleStructure of the BMAL1/HIF2A heterodimer in Complex with DNA
Keywords keywordsTranscriptional factors, heterodimer, DNA recognition, Circadian-dependent cardioprotection, TRANSCRIPTION-DNA complex; TRANSCRIPTION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.15
Radius of gyration Rg (electron density) rg_electron33.73
Forward intensity I(0) i091855900.00
Molecular weight molecular_weight67761.0 kDa
Excluded volume excluded_volume81451 ų
Envelope volume envelope_volume125970 ų
Hydration-shell volume shell_volume33916 ų
Envelope diameter envelope_diameter119.0
Shell Rg shell_rg37.20
Envelope Rg envelope_rg33.59
Shape Rg shape_rg33.68
Total Rg total_rg34.16
Total atoms total_atoms4719
Residues n_residues548
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 dmax119.2
Rg (real space) rg_real35.36
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real9.1860e+07
I(0) uncertainty (real space) i0_real_error1.6910e+06
Rg (reciprocal space) rg_reciprocal35.23
I(0) (reciprocal space) i0_reciprocal91840000.0000
Solution quality estimate total_estimate0.8564
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.4
Skewness Skewness skewness0.419
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8398000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.822; Smooth: 0.799

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)