8js9

Cryo-EM structure of SV2A in complex with BoNT/A2 Hc

Method: ELECTRON MICROSCOPY Dmax: 144.8 Å Quality: GOOD

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 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–742 Not recorded Botulinum neurotoxin × 1 (D2KCK3) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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 10–750; UniProt 2–742

Botulinum neurotoxin

Clostridium botulinum

UniProt D2KCK3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 871–1296 Not recorded Synaptic vesicle glycoprotein 2A × 1 (Q7L0J3) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.01 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D2KCK3_CLOBO
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–426; UniProt 871–1296

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 8js9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8js9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8js9
Deposition date deposition_date2023-06-19
Structure title titleCryo-EM structure of SV2A in complex with BoNT/A2 Hc
Keywords keywordsSynaptic vesicle, botulinum neurotoxin, epilepsy, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.72
Radius of gyration Rg (electron density) rg_electron42.37
Forward intensity I(0) i0187765000.00
Molecular weight molecular_weight115970.0 kDa
Excluded volume excluded_volume146640 ų
Envelope volume envelope_volume201570 ų
Hydration-shell volume shell_volume40760 ų
Envelope diameter envelope_diameter144.0
Shell Rg shell_rg45.95
Envelope Rg envelope_rg41.29
Shape Rg shape_rg42.33
Total Rg total_rg42.70
Total atoms total_atoms8177
Residues n_residues1012
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 dmax144.8
Rg (real space) rg_real42.97
Rg uncertainty (real space) rg_real_error1.58
I(0) (real space) i0_real1.8780e+08
I(0) uncertainty (real space) i0_real_error3.4340e+06
Rg (reciprocal space) rg_reciprocal42.72
I(0) (reciprocal space) i0_reciprocal187700000.0000
Solution quality estimate total_estimate0.8154
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.3
Skewness Skewness skewness0.333
Kurtosis Kurtosis kurtosis-0.790
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16750000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.703; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.686; Smooth: 0.802

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)