9ct6

HsSTING with diABZI and C53, apart conformation

Method: ELECTRON MICROSCOPY Dmax: 204.4 Å Quality: GOOD

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

Stimulator of interferon genes protein

Homo sapiens

UniProt Q86WV6

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–344 Chain B; UniProt 1–344 Chain C; UniProt 1–344 Chain D; UniProt 1–344 Chain E; UniProt 1–344 Chain F; UniProt 1–344 Chain G; UniProt 1–344 Chain H; UniProt 1–344 Chain I; UniProt 1–344 Chain J; UniProt 1–344 Chain K; UniProt 1–344 Chain L; UniProt 1–344 Not recorded A1AZ0 1-[(2E)-4-{5-carbamoyl-2-[(1-ethyl-3-methyl-1H-pyrazole-5-carbonyl)amino]-7-methoxy-1H-1,3-benzimidazol-1-yl}but-2-en-1-yl]-2-[(1-ethyl-3-methyl-1H-pyrazole-5-carbonyl)amino]-7-[3-(morpholin-4-yl)propoxy]-1H-1,3-benzimidazole-5-carboxamide × 6 9IM 1-[(2-chloro-6-fluorophenyl)methyl]-3,3-dimethyl-2-oxo-N-[(2,4,6-trifluorophenyl)methyl]-2,3-dihydro-1H-indole-6-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.56 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.

84 other PDB entries and 90 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STING_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–344; UniProt 1–344 Author chain B; PDBConstruct 1–344; UniProt 1–344 Author chain C; PDBConstruct 1–344; UniProt 1–344 Author chain D; PDBConstruct 1–344; UniProt 1–344 Author chain E; PDBConstruct 1–344; UniProt 1–344 Author chain F; PDBConstruct 1–344; UniProt 1–344 Author chain G; PDBConstruct 1–344; UniProt 1–344 Author chain H; PDBConstruct 1–344; UniProt 1–344 Author chain I; PDBConstruct 1–344; UniProt 1–344 Author chain J; PDBConstruct 1–344; UniProt 1–344 Author chain K; PDBConstruct 1–344; UniProt 1–344 Author chain L; PDBConstruct 1–344; UniProt 1–344

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 9ct6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ct6
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9ct6
Deposition date deposition_date2024-07-24
最后修订 last_revision2025-04-23
Structure title titleHsSTING with diABZI and C53, apart conformation
Keywords keywordsInnate immunity, membrane protein, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.63
Radius of gyration Rg (electron density) rg_electron59.20
Forward intensity I(0) i04907060000.00
Molecular weight molecular_weight392780.0 kDa
Excluded volume excluded_volume381610 ų
Envelope volume envelope_volume802860 ų
Hydration-shell volume shell_volume114860 ų
Envelope diameter envelope_diameter201.5
Shell Rg shell_rg58.99
Envelope Rg envelope_rg57.98
Shape Rg shape_rg59.25
Total Rg total_rg59.11
Total atoms total_atoms29814
Residues n_residues3702
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 dmax204.4
Rg (real space) rg_real58.66
Rg uncertainty (real space) rg_real_error2.24
I(0) (real space) i0_real4.9070e+09
I(0) uncertainty (real space) i0_real_error1.0380e+08
Rg (reciprocal space) rg_reciprocal58.58
I(0) (reciprocal space) i0_reciprocal4906000000.0000
Solution quality estimate total_estimate0.8642
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.6
Skewness Skewness skewness0.310
Kurtosis Kurtosis kurtosis-0.484
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha415600000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.820; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.786

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)