4ef5

Crystal structure of STING CTD

Method: X-RAY DIFFRACTION Dmax: 60.5 Å Quality: GOOD

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

Transmembrane protein 173

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 139–379 Fragment:C-TERMINAL DOMAIN No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;14.4%(w/v) PEG8000, 0.08M Cacodylate, 0.16M calcium acetate, 20%(v/v) glycerol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.45 Å R-free 0.288

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 TM173_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 25–265; UniProt 139–379

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 4ef5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ef5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4ef5
Deposition date deposition_date2012-03-29
Structure title titleCrystal structure of STING CTD
Keywords keywords;STING/MITA/ERIS/MPYS/TMEM173, innate immune system, type I interferon, dimerization, c-di-GMP, 5 helices and 5 strands in single domain, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.23
Radius of gyration Rg (electron density) rg_electron16.92
Forward intensity I(0) i07896540.00
Molecular weight molecular_weight20332.0 kDa
Excluded volume excluded_volume25384 ų
Envelope volume envelope_volume29776 ų
Hydration-shell volume shell_volume15179 ų
Envelope diameter envelope_diameter62.2
Shell Rg shell_rg22.47
Envelope Rg envelope_rg17.20
Shape Rg shape_rg16.93
Total Rg total_rg17.86
Total atoms total_atoms1433
Residues n_residues177
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 dmax60.5
Rg (real space) rg_real18.19
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real7.8970e+06
I(0) uncertainty (real space) i0_real_error9.9700e+04
Rg (reciprocal space) rg_reciprocal18.20
I(0) (reciprocal space) i0_reciprocal7897000.0000
Solution quality estimate total_estimate0.8018
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.9
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.180
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1427000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4ef5a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.387 — STING C-terminal-like
Superfamily Superfamily superfamilyd.387.1 — STING, TM173 CTD-like
Family Family familyd.387.1.1 — Tyrosinase cofactor MelC1

CATH v4.4 (2 domains)

Domain ID domain_id4ef5A01
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 superfamily5200
Domain ID domain_id4ef5A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily12100 — Stimulator of interferon genes protein

8. Citations (1)

9. Files and Curves (10)