9pff

Min22bin20S complex (NSF-alphaSNAP-2:2 syntaxin-1a H3:SNAP-25 SN1), non-hydrolyzing, class 27

Method: ELECTRON MICROSCOPY Dmax: 230.1 Å Quality: GOOD

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

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain G; UniProt 1–83 Chain I; UniProt 1–83 Not recorded Syntaxin-1A × 2 (P32851) Alpha-soluble NSF attachment protein × 4 (P54921) 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 3.09 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 1
Chains and sequence ranges Author chain G; PDBConstruct 2–84; UniProt 1–83 Author chain I; PDBConstruct 2–84; UniProt 1–83

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain H; UniProt 191–267 Chain J; UniProt 191–267 Not recorded Synaptosomal-associated protein 25 × 2 (P60881) Alpha-soluble NSF attachment protein × 4 (P54921) 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 3.09 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 H; PDBConstruct 2–78; UniProt 191–267 Author chain J; PDBConstruct 2–78; UniProt 191–267

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain L; UniProt 1–295 Chain M; UniProt 1–295 Chain N; UniProt 1–295 Chain O; UniProt 1–295 Not recorded Synaptosomal-associated protein 25 × 2 (P60881) Syntaxin-1A × 2 (P32851) 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 3.09 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 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 Author chain O; PDBConstruct 2–296; UniProt 1–295

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 × 14 PDB declaration: tetradecameric(14) 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 × 2 (P60881) Syntaxin-1A × 2 (P32851) Alpha-soluble NSF attachment protein × 4 (P54921) ATP ADENOSINE-5'-TRIPHOSPHATE × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.09 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 4
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

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 9pff

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9pff
Deposition date deposition_date2025-07-04
Structure title titleMin22bin20S complex (NSF-alphaSNAP-2:2 syntaxin-1a H3:SNAP-25 SN1), non-hydrolyzing, class 27
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_guinier64.75
Radius of gyration Rg (electron density) rg_electron64.59
Forward intensity I(0) i04452460000.00
Molecular weight molecular_weight559520.0 kDa
Excluded volume excluded_volume699740 ų
Envelope volume envelope_volume1124000 ų
Hydration-shell volume shell_volume144440 ų
Envelope diameter envelope_diameter218.1
Shell Rg shell_rg67.88
Envelope Rg envelope_rg62.12
Shape Rg shape_rg64.59
Total Rg total_rg64.62
Total atoms total_atoms78684
Residues n_residues4964
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 dmax230.1
Rg (real space) rg_real64.78
Rg uncertainty (real space) rg_real_error2.10
I(0) (real space) i0_real4.4530e+09
I(0) uncertainty (real space) i0_real_error9.1280e+07
Rg (reciprocal space) rg_reciprocal64.71
I(0) (reciprocal space) i0_reciprocal4452000000.0000
Solution quality estimate total_estimate0.8581
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary67.1
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.378
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0034
Highest regularization parameter α highest_alpha467500000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.766; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.857

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (2)

9. Files and Curves (10)