9oju

21bin20S complex (NSF-alphaSNAP-2:1 syntaxin-1a:SNAP-25), non-hydrolyzing, class 4

Method: ELECTRON MICROSCOPY Dmax: 151.8 Å Quality: GOOD

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

Vesicle-fusing ATPase

Cricetulus griseus

UniProt P18708

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–744 Chain B; UniProt 1–744 Chain C; UniProt 1–744 Chain D; UniProt 1–744 Chain E; UniProt 1–744 Chain F; UniProt 1–744 Not recorded Synaptosomal-associated protein 25 × 1 (P60881) ATP ADENOSINE-5'-TRIPHOSPHATE × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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.

41 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NSF_CRIGR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–747; UniProt 1–744 Author chain B; PDBConstruct 4–747; UniProt 1–744 Author chain C; PDBConstruct 4–747; UniProt 1–744 Author chain D; PDBConstruct 4–747; UniProt 1–744 Author chain E; PDBConstruct 4–747; UniProt 1–744 Author chain F; PDBConstruct 4–747; UniProt 1–744

Synaptosomal-associated protein 25

Rattus norvegicus

UniProt P60881

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain H; UniProt 1–83 Not recorded Vesicle-fusing ATPase × 6 (P18708) ATP ADENOSINE-5'-TRIPHOSPHATE × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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.

39 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNP25_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 2–84; UniProt 1–83

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 9oju

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9oju
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9oju
Deposition date deposition_date2025-05-08
Structure title title21bin20S complex (NSF-alphaSNAP-2:1 syntaxin-1a:SNAP-25), non-hydrolyzing, class 4
Keywords keywords;ATPase, SNARE, hydrolysis, disassembly, translocation, exocytosis, neurotransmitter release, synapse, synaptic transmission, membrane fusion, HYDROLASE ;; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.42
Radius of gyration Rg (electron density) rg_electron48.51
Forward intensity I(0) i01871780000.00
Molecular weight molecular_weight359870.0 kDa
Excluded volume excluded_volume451230 ų
Envelope volume envelope_volume687800 ų
Hydration-shell volume shell_volume113160 ų
Envelope diameter envelope_diameter154.7
Shell Rg shell_rg57.22
Envelope Rg envelope_rg46.77
Shape Rg shape_rg48.54
Total Rg total_rg48.71
Total atoms total_atoms50964
Residues n_residues3190
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 dmax151.8
Rg (real space) rg_real48.93
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real1.8720e+09
I(0) uncertainty (real space) i0_real_error3.4150e+07
Rg (reciprocal space) rg_reciprocal49.41
I(0) (reciprocal space) i0_reciprocal1873000000.0000
Solution quality estimate total_estimate0.8856
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary66.4
Skewness Skewness skewness0.015
Kurtosis Kurtosis kurtosis-0.517
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha200800000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.889

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)