9om6

22bin20S complex (NSF-alphaSNAP-2:2 syntaxin-1a:SNAP-25), 4:2:2 alphaSNAP-syntaxin-1a-SNAP-25 subcomplex local refinement, hydrolyzing, class 23

Method: ELECTRON MICROSCOPY Dmax: 112.3 Å Quality: GOOD

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

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–267 Chain B; UniProt 1–267 Not recorded Synaptosomal-associated protein 25 × 2 (P60881) Alpha-soluble NSF attachment protein × 4 (P54921) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–267; UniProt 1–267 Author chain B; 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–206 Chain D; UniProt 1–206 Not recorded Syntaxin-1A × 2 (P32851) Alpha-soluble NSF attachment protein × 4 (P54921) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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 C; PDBConstruct 17–222; UniProt 1–206 Author chain D; 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–295 Chain F; UniProt 1–295 Chain G; UniProt 1–295 Chain H; UniProt 1–295 Not recorded Syntaxin-1A × 2 (P32851) Synaptosomal-associated protein 25 × 2 (P60881) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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 3
Chains and sequence ranges Author chain E; PDBConstruct 2–296; UniProt 1–295 Author chain F; PDBConstruct 2–296; UniProt 1–295 Author chain G; PDBConstruct 2–296; UniProt 1–295 Author chain H; 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 9om6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9om6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9om6
Deposition date deposition_date2025-05-13
Structure title title22bin20S complex (NSF-alphaSNAP-2:2 syntaxin-1a:SNAP-25), 4:2:2 alphaSNAP-syntaxin-1a-SNAP-25 subcomplex local refinement, hydrolyzing, class 23
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_guinier36.23
Radius of gyration Rg (electron density) rg_electron35.48
Forward intensity I(0) i0414080000.00
Molecular weight molecular_weight160780.0 kDa
Excluded volume excluded_volume199930 ų
Envelope volume envelope_volume282810 ų
Hydration-shell volume shell_volume64194 ų
Envelope diameter envelope_diameter115.0
Shell Rg shell_rg43.55
Envelope Rg envelope_rg34.80
Shape Rg shape_rg35.48
Total Rg total_rg36.07
Total atoms total_atoms22312
Residues n_residues1426
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 dmax112.3
Rg (real space) rg_real36.00
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real4.1410e+08
I(0) uncertainty (real space) i0_real_error6.5020e+06
Rg (reciprocal space) rg_reciprocal36.14
I(0) (reciprocal space) i0_reciprocal414100000.0000
Solution quality estimate total_estimate0.8874
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.0
Skewness Skewness skewness0.146
Kurtosis Kurtosis kurtosis-0.397
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha84430000.0000
Real-space data points n_real_points45
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: 0.969; Smooth: 0.889

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (2)

9. Files and Curves (10)