9pc9

Structure of Synaptic Vesicle Protein 2A Bound to UCB7361

Method: ELECTRON MICROSCOPY Dmax: 84.8 Å Quality: REASONABLE

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

Synaptic vesicle glycoprotein 2A

Homo sapiens

UniProt Q7L0J3

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–742 Not recorded A1CHN (4S)-1-{[(4S)-2-(methoxymethyl)-6-(trifluoromethyl)imidazo[2,1-b][1,3,4]thiadiazol-5-yl]methyl}-4-(3,3,3-trifluoropropyl)pyrrolidin-2-one × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.91 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SV2A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–742; UniProt 1–742

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 9pc9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pc9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9pc9
Deposition date deposition_date2025-06-27
Structure title titleStructure of Synaptic Vesicle Protein 2A Bound to UCB7361
Keywords keywordsSynaptic vesicle, SLC22, Inhibitor, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier22.53
Radius of gyration Rg (electron density) rg_electron21.37
Forward intensity I(0) i033089800.00
Molecular weight molecular_weight47313.0 kDa
Excluded volume excluded_volume60246 ų
Envelope volume envelope_volume67332 ų
Hydration-shell volume shell_volume25626 ų
Envelope diameter envelope_diameter80.9
Shell Rg shell_rg28.99
Envelope Rg envelope_rg22.04
Shape Rg shape_rg21.30
Total Rg total_rg22.54
Total atoms total_atoms6600
Residues n_residues435
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 dmax84.8
Rg (real space) rg_real22.50
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real3.3090e+07
I(0) uncertainty (real space) i0_real_error4.8440e+05
Rg (reciprocal space) rg_reciprocal22.51
I(0) (reciprocal space) i0_reciprocal33090000.0000
Solution quality estimate total_estimate0.7455
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.355
Kurtosis Kurtosis kurtosis-0.206
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8514000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.585; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.935; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)