9ojz

21bin20S complex (NSF-alphaSNAP-2:1 syntaxin-1a:SNAP-25), non-hydrolyzing, class 5

Method: ELECTRON MICROSCOPY Dmax: 236.0 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 × 12 PDB declaration: dodecameric(12) 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 Syntaxin-1A × 2 (P32851) Synaptosomal-associated protein 25 × 1 (P60881) Alpha-soluble NSF attachment protein × 3 (P54921) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 11 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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

Syntaxin-1A

Rattus norvegicus

UniProt P32851

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain G; UniProt 1–267 Chain H; UniProt 1–267 Not recorded Vesicle-fusing ATPase × 6 (P18708) Synaptosomal-associated protein 25 × 1 (P60881) Alpha-soluble NSF attachment protein × 3 (P54921) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 11 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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.

53 other PDB entries and 72 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STX1A_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–267; UniProt 1–267 Author chain H; PDBConstruct 1–267; UniProt 1–267

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain I; UniProt 1–206 Not recorded Vesicle-fusing ATPase × 6 (P18708) Syntaxin-1A × 2 (P32851) Alpha-soluble NSF attachment protein × 3 (P54921) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 11 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 3
Chains and sequence ranges Author chain I; PDBConstruct 17–222; UniProt 1–206

Alpha-soluble NSF attachment protein

Rattus norvegicus

UniProt P54921

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain J; UniProt 1–295 Chain K; UniProt 1–295 Chain L; UniProt 1–295 Not recorded Vesicle-fusing ATPase × 6 (P18708) Syntaxin-1A × 2 (P32851) Synaptosomal-associated protein 25 × 1 (P60881) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 11 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNAA_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain J; PDBConstruct 2–296; UniProt 1–295 Author chain K; PDBConstruct 2–296; UniProt 1–295 Author chain L; PDBConstruct 2–296; UniProt 1–295

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 9ojz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ojz
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9ojz
Deposition date deposition_date2025-05-08
Structure title title21bin20S complex (NSF-alphaSNAP-2:1 syntaxin-1a:SNAP-25), non-hydrolyzing, class 5
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_guinier66.41
Radius of gyration Rg (electron density) rg_electron66.20
Forward intensity I(0) i05043430000.00
Molecular weight molecular_weight595840.0 kDa
Excluded volume excluded_volume745000 ų
Envelope volume envelope_volume1249200 ų
Hydration-shell volume shell_volume156150 ų
Envelope diameter envelope_diameter223.6
Shell Rg shell_rg70.57
Envelope Rg envelope_rg63.39
Shape Rg shape_rg66.20
Total Rg total_rg66.26
Total atoms total_atoms83855
Residues n_residues5291
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 dmax236.0
Rg (real space) rg_real66.32
Rg uncertainty (real space) rg_real_error2.09
I(0) (real space) i0_real5.0440e+09
I(0) uncertainty (real space) i0_real_error1.1020e+08
Rg (reciprocal space) rg_reciprocal66.48
I(0) (reciprocal space) i0_reciprocal5045000000.0000
Solution quality estimate total_estimate0.8482
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary78.7
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.251
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0040
Highest regularization parameter α highest_alpha390600000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.727; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.855

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (2)

9. Files and Curves (10)