9dh3

Cryo-EM structure of NLRP3 complex with Compound C

Method: ELECTRON MICROSCOPY Dmax: 182.9 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,NACHT, LRR and PYD domains-containing protein 3 chimera

Homo sapiens

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 27–392 Chain B; UniProt 27–392 Chain C; UniProt 27–392 Chain D; UniProt 27–392 Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 4 A1A4L 2-[(4S)-5-ethyl-8-oxothieno[2',3':4,5]pyrrolo[1,2-d][1,2,4]triazin-7(8H)-yl]-N-(pyrimidin-4-yl)acetamide × 4 CPS 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.76 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–366; UniProt 27–392 Author chain B; PDBConstruct 1–366; UniProt 27–392 Author chain C; PDBConstruct 1–366; UniProt 27–392 Author chain D; PDBConstruct 1–366; UniProt 27–392

Maltose/maltodextrin-binding periplasmic protein,NACHT, LRR and PYD domains-containing protein 3 chimera

Homo sapiens

UniProt Q96P20

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 136–1036 Chain B; UniProt 136–1036 Chain C; UniProt 136–1036 Chain D; UniProt 136–1036 Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 4 A1A4L 2-[(4S)-5-ethyl-8-oxothieno[2',3':4,5]pyrrolo[1,2-d][1,2,4]triazin-7(8H)-yl]-N-(pyrimidin-4-yl)acetamide × 4 CPS 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.76 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.

23 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NLRP3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 367–1267; UniProt 136–1036 Author chain B; PDBConstruct 367–1267; UniProt 136–1036 Author chain C; PDBConstruct 367–1267; UniProt 136–1036 Author chain D; PDBConstruct 367–1267; UniProt 136–1036

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 9dh3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9dh3
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9dh3
Deposition date deposition_date2024-09-03
Structure title titleCryo-EM structure of NLRP3 complex with Compound C
Keywords keywordsNLRP3 Inflammasome, Small Molecule Inhibitors, and Drug Discovery, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.95
Radius of gyration Rg (electron density) rg_electron65.56
Forward intensity I(0) i07871900000.00
Molecular weight molecular_weight499380.0 kDa
Excluded volume excluded_volume484560 ų
Envelope volume envelope_volume1033000 ų
Hydration-shell volume shell_volume131950 ų
Envelope diameter envelope_diameter196.0
Shell Rg shell_rg69.66
Envelope Rg envelope_rg62.13
Shape Rg shape_rg65.63
Total Rg total_rg65.48
Total atoms total_atoms37752
Residues n_residues4724
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 dmax182.9
Rg (real space) rg_real65.43
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real7.8720e+09
I(0) uncertainty (real space) i0_real_error1.5570e+08
Rg (reciprocal space) rg_reciprocal66.36
I(0) (reciprocal space) i0_reciprocal7884000000.0000
Solution quality estimate total_estimate0.8278
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary83.8
Skewness Skewness skewness0.049
Kurtosis Kurtosis kurtosis-0.374
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha125800000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.004

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)