9pd8

22bin20S complex (NSF-alphaSNAP-2:2 syntaxin-1a:SNAP-25), hydrolyzing, class 21

Method: ELECTRON MICROSCOPY Dmax: 218.9 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 × 15 PDB declaration: pentadecameric(15) 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,Synaptosomal-associated protein 25,Synaptosomal-associated protein 25,Alpha-soluble NSF attachment protein ; × 2 (P60881) Syntaxin-1A × 2 (P32851) Alpha-soluble NSF attachment protein isoform X2 × 4 (A0A8C2LIB4) unknown sequence × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.23 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,Synaptosomal-associated protein 25,Synaptosomal-associated protein 25,Alpha-soluble NSF attachment protein ;

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain I; UniProt 1–206 Chain J; UniProt 1–206 Not recorded Vesicle-fusing ATPase × 6 (P18708) Syntaxin-1A × 2 (P32851) Alpha-soluble NSF attachment protein isoform X2 × 4 (A0A8C2LIB4) unknown sequence × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.23 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 I; PDBConstruct 17–222; UniProt 1–206 Author chain J; PDBConstruct 17–222; UniProt 1–206

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 × 15 PDB declaration: pentadecameric(15) 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,Synaptosomal-associated protein 25,Synaptosomal-associated protein 25,Alpha-soluble NSF attachment protein ; × 2 (P60881) Alpha-soluble NSF attachment protein isoform X2 × 4 (A0A8C2LIB4) unknown sequence × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.23 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 3
Chains and sequence ranges Author chain G; PDBConstruct 1–267; UniProt 1–267 Author chain H; PDBConstruct 1–267; UniProt 1–267

Alpha-soluble NSF attachment protein isoform X2

Cricetulus griseus

UniProt A0A8C2LIB4

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain K; UniProt 1–295 Chain L; UniProt 1–295 Chain M; UniProt 1–295 Chain N; UniProt 1–295 Not recorded Vesicle-fusing ATPase × 6 (P18708) ;Synaptosomal-associated protein 25,Synaptosomal-associated protein 25,Synaptosomal-associated protein 25,Alpha-soluble NSF attachment protein ; × 2 (P60881) Syntaxin-1A × 2 (P32851) unknown sequence × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A8C2LIB4_CRIGR
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 2–296; UniProt 1–295 Author chain L; PDBConstruct 2–296; UniProt 1–295 Author chain M; PDBConstruct 2–296; UniProt 1–295 Author chain N; 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 9pd8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pd8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9pd8
Deposition date deposition_date2025-06-30
Structure title title22bin20S complex (NSF-alphaSNAP-2:2 syntaxin-1a:SNAP-25), hydrolyzing, class 21
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_guinier63.84
Radius of gyration Rg (electron density) rg_electron63.49
Forward intensity I(0) i05170140000.00
Molecular weight molecular_weight604250.0 kDa
Excluded volume excluded_volume755950 ų
Envelope volume envelope_volume1221200 ų
Hydration-shell volume shell_volume157390 ų
Envelope diameter envelope_diameter211.4
Shell Rg shell_rg69.19
Envelope Rg envelope_rg60.88
Shape Rg shape_rg63.50
Total Rg total_rg63.55
Total atoms total_atoms85007
Residues n_residues5374
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 dmax218.9
Rg (real space) rg_real63.64
Rg uncertainty (real space) rg_real_error1.63
I(0) (real space) i0_real5.1700e+09
I(0) uncertainty (real space) i0_real_error1.0900e+08
Rg (reciprocal space) rg_reciprocal64.00
I(0) (reciprocal space) i0_reciprocal5173000000.0000
Solution quality estimate total_estimate0.8585
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary78.8
Skewness Skewness skewness0.271
Kurtosis Kurtosis kurtosis-0.323
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0029
Highest regularization parameter α highest_alpha520200000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.829

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (2)

9. Files and Curves (10)