5cci

Structure of the Mg2+-bound synaptotagmin-1 SNARE complex (short unit cell form)

Method: X-RAY DIFFRACTION Dmax: 134.8 Å Quality: GOOD

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

Vesicle-associated membrane protein 2

Rattus norvegicus

UniProt P63045

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 28–89 Fragment:UNP residues 28-89 Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 (P60881) Synaptosomal-associated protein 25 × 1 (P60881) Synaptotagmin-1 × 3 (P21707) MG MAGNESIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;0.75% v/v PEG3350, 25 mM HEPES-Na, 75 mM NaCl, 25 mM MgCl2 Resolution 4.10 Å R-free 0.323

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.

22 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VAMP2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–63; UniProt 28–89

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 191–256 Fragment:UNP residues 191-256 Vesicle-associated membrane protein 2 × 1 (P63045) Synaptosomal-associated protein 25 × 1 (P60881) Synaptosomal-associated protein 25 × 1 (P60881) Synaptotagmin-1 × 3 (P21707) MG MAGNESIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;0.75% v/v PEG3350, 25 mM HEPES-Na, 75 mM NaCl, 25 mM MgCl2 Resolution 4.10 Å R-free 0.323

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 2–67; UniProt 191–256

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 7–83 Chain D; UniProt 141–204 Fragment:UNP residues 7-83 Fragment:UNP residues 141-204 Vesicle-associated membrane protein 2 × 1 (P63045) Syntaxin-1A × 1 (P32851) Synaptotagmin-1 × 3 (P21707) MG MAGNESIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;0.75% v/v PEG3350, 25 mM HEPES-Na, 75 mM NaCl, 25 mM MgCl2 Resolution 4.10 Å R-free 0.323

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 P60881-2
PDB entities 3, 4
Chains and sequence ranges Author chain C; PDBConstruct 1–77; UniProt 7–83 Author chain D; PDBConstruct 2–65; UniProt 141–204

Synaptotagmin-1

Rattus norvegicus

UniProt P21707

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain E; UniProt 141–421 Chain F; UniProt 141–421 Fragment:UNP residues 141-421 Vesicle-associated membrane protein 2 × 1 (P63045) Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 (P60881) Synaptosomal-associated protein 25 × 1 (P60881) MG MAGNESIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;0.75% v/v PEG3350, 25 mM HEPES-Na, 75 mM NaCl, 25 mM MgCl2 Resolution 4.10 Å R-free 0.323

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.

19 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYT1_RAT
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–281; UniProt 141–421 Author chain F; PDBConstruct 1–281; UniProt 141–421

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 5cci

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5cci
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5cci
Deposition date deposition_date2015-07-02
Structure title titleStructure of the Mg2+-bound synaptotagmin-1 SNARE complex (short unit cell form)
Keywords keywordssynaptic fusion complex, Synaptotagmin1, neuronal SNARE complex, ENDOCYTOSIS, EXOCYTOSIS; ENDOCYTOSIS,EXOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.19
Radius of gyration Rg (electron density) rg_electron41.57
Forward intensity I(0) i0131275000.00
Molecular weight molecular_weight91116.0 kDa
Excluded volume excluded_volume113510 ų
Envelope volume envelope_volume174190 ų
Hydration-shell volume shell_volume37855 ų
Envelope diameter envelope_diameter138.1
Shell Rg shell_rg42.61
Envelope Rg envelope_rg41.00
Shape Rg shape_rg41.62
Total Rg total_rg41.48
Total atoms total_atoms6406
Residues n_residues814
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 dmax134.8
Rg (real space) rg_real41.34
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real1.3130e+08
I(0) uncertainty (real space) i0_real_error2.5500e+06
Rg (reciprocal space) rg_reciprocal41.19
I(0) (reciprocal space) i0_reciprocal131300000.0000
Solution quality estimate total_estimate0.8656
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.1
Skewness Skewness skewness0.309
Kurtosis Kurtosis kurtosis-0.693
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4331000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.844; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 0.793

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)