9wsr

Structure of mouse NLRP14-KDM2A-SKP1 complex

Method: ELECTRON MICROSCOPY Dmax: 118.3 Å Quality: EXCELLENT

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

Lysine-specific demethylase 2A

Mus musculus

UniProt P59997

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 815–1161 Not recorded S-phase kinase-associated protein 1 × 1 (Q9WTX5) NACHT, LRR and PYD domains-containing protein 14 × 1 (Q6B966) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDM2A_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 12–358; UniProt 815–1161

S-phase kinase-associated protein 1

Mus musculus

UniProt Q9WTX5

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–163 Not recorded Lysine-specific demethylase 2A × 1 (P59997) NACHT, LRR and PYD domains-containing protein 14 × 1 (Q6B966) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKP1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 12–174; UniProt 1–163

NACHT, LRR and PYD domains-containing protein 14

Mus musculus

UniProt Q6B966

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–993 Not recorded Lysine-specific demethylase 2A × 1 (P59997) S-phase kinase-associated protein 1 × 1 (Q9WTX5) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NAL14_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 21–1013; UniProt 1–993

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 9wsr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9wsr
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9wsr
Deposition date deposition_date2025-09-15
Structure title titleStructure of mouse NLRP14-KDM2A-SKP1 complex
Keywords keywordsCryo-EM, Complex, early embryonic development, NLRP14, KDM2A, SKP1, ubiquitylation., CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.74
Radius of gyration Rg (electron density) rg_electron39.07
Forward intensity I(0) i0276838000.00
Molecular weight molecular_weight134470.0 kDa
Excluded volume excluded_volume168400 ų
Envelope volume envelope_volume244590 ų
Hydration-shell volume shell_volume52194 ų
Envelope diameter envelope_diameter119.9
Shell Rg shell_rg44.92
Envelope Rg envelope_rg38.08
Shape Rg shape_rg39.10
Total Rg total_rg39.33
Total atoms total_atoms9408
Residues n_residues1192
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 dmax118.3
Rg (real space) rg_real39.52
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real2.7680e+08
I(0) uncertainty (real space) i0_real_error5.3500e+06
Rg (reciprocal space) rg_reciprocal39.66
I(0) (reciprocal space) i0_reciprocal276900000.0000
Solution quality estimate total_estimate0.9105
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.2
Skewness Skewness skewness0.033
Kurtosis Kurtosis kurtosis-0.784
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33970000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.985; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.878

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)