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6nt6

Cryo-EM structure of full-length chicken STING in the apo state

Method: ELECTRON MICROSCOPY Dmax: 93.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Stimulator of interferon genes protein

Gallus gallus

UniProt A0A1D5P7Q9

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–379 Chain B； UniProt 1–379 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 4.00 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.

Other PDB Difference from Current Entry 6NT6 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6NT7 Cryo-EM structure of full-length chicken STING in the cGAMP-bound dimeric state Deposited 2019-01-28 Different ligand/ion Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–379（379 aa）
Chain B 1–379（379 aa）
Not recorded 1SY cGAMP × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å
6NT8 Cryo-EM structure of full-length chicken STING in the cGAMP-bound tetrameric state Deposited 2019-01-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–379（379 aa）
Chain B 1–379（379 aa）
Chain D 1–379（379 aa）
Chain E 1–379（379 aa）
Not recorded 1SY cGAMP × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.50 Å
6NT9 Cryo-EM structure of the complex between human TBK1 and chicken STING Deposited 2019-01-28 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–379（379 aa）
Chain D 1–379（379 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å

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

View Construct and Data Evidence
UniProt name A0A1D5P7Q9_CHICK
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–379； UniProt 1–379 Author chain B； PDBConstruct 1–379； UniProt 1–379

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 6nt6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6nt6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6nt6
Deposition date deposition_date2019-01-28
Structure title titleCryo-EM structure of full-length chicken STING in the apo state
Keywords keywordsER, membrane, adaptor, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier28.89 Å
Radius of gyration Rg (electron density) rg_electron28.70 Å
Forward intensity I(0) i054897800.00
Molecular weight molecular_weight59819.0 kDa
Excluded volume excluded_volume75947 ų
Envelope volume envelope_volume105970 ų
Hydration-shell volume shell_volume31656 ų
Envelope diameter envelope_diameter98.2 Å
Shell Rg shell_rg35.05 Å
Envelope Rg envelope_rg28.61 Å
Shape Rg shape_rg28.68 Å
Total Rg total_rg29.46 Å
Total atoms total_atoms4198
Residues n_residues556
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax93.2 Å
Rg (real space) rg_real28.90 Å
Rg uncertainty (real space) rg_real_error0.76 Å
I(0) (real space) i0_real5.4900e+07
I(0) uncertainty (real space) i0_real_error9.1070e+05
Rg (reciprocal space) rg_reciprocal28.90 Å
I(0) (reciprocal space) i0_reciprocal54900000.0000
Solution quality estimate total_estimate0.8976
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.2 Å
Skewness Skewness skewness0.345
Kurtosis Kurtosis kurtosis-0.389
Angular range angular_range— – 0.2750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8788000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.951
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)