7udc

cryo-EM structures of a synaptobrevin-Munc18-1-syntaxin-1 complex class1

Method: ELECTRON MICROSCOPY Dmax: 107.4 Å Quality: REASONABLE

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

Syntaxin-binding protein 1

Rattus norvegicus

UniProt P61765

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–594 Mutation:D326K Syntaxin-1A × 1 (P32851) Synaptobrevin-2 × 1 (P63027) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STXB1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–607; UniProt 1–594

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 2–253 Mutation:C145A, L165A, E166A, L205C Syntaxin-binding protein 1 × 1 (P61765) Synaptobrevin-2 × 1 (P63027) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 B; PDBConstruct 3–254; UniProt 2–253

Synaptobrevin-2

Rattus norvegicus

UniProt P63027

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 29–83 Mutation:Q36C Syntaxin-binding protein 1 × 1 (P61765) Syntaxin-1A × 1 (P32851) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

6 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VAMP2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 5–59; UniProt 29–83

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 7udc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7udc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7udc
Deposition date deposition_date2022-03-18
Structure title titlecryo-EM structures of a synaptobrevin-Munc18-1-syntaxin-1 complex class1
Keywords keywordsMunc18, syntaxin, synaptobrevin, SNARE, membrane fusion, neurotransmitter release, EXOCYTOSIS; EXOCYTOSIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.33
Radius of gyration Rg (electron density) rg_electron31.43
Forward intensity I(0) i0135808000.00
Molecular weight molecular_weight91616.0 kDa
Excluded volume excluded_volume114550 ų
Envelope volume envelope_volume155280 ų
Hydration-shell volume shell_volume40925 ų
Envelope diameter envelope_diameter113.0
Shell Rg shell_rg38.48
Envelope Rg envelope_rg31.57
Shape Rg shape_rg31.43
Total Rg total_rg32.07
Total atoms total_atoms6425
Residues n_residues806
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 dmax107.4
Rg (real space) rg_real32.28
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real1.3580e+08
I(0) uncertainty (real space) i0_real_error2.2720e+06
Rg (reciprocal space) rg_reciprocal32.31
I(0) (reciprocal space) i0_reciprocal135800000.0000
Solution quality estimate total_estimate0.7206
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.3
Skewness Skewness skewness0.270
Kurtosis Kurtosis kurtosis-0.465
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37960000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.996; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7udcA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2060 — Sec1/Munc18 (SM) protein, domain 1
Domain ID domain_id7udcA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology830 — Syntaxin Binding Protein 1; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Sec1/Munc18 (SM) protein, domain 3a

8. Citations (1)

9. Files and Curves (10)