5w5c

Crystal structure of the primed SNARE-Complexin-Synaptotagmin-1 C2AB complex

Method: X-RAY DIFFRACTION Dmax: 97.7 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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 28–66 Fragment:UNP residues 29-66 Syntaxin-1A × 2 (P32851) Synaptosomal-associated protein 25 × 2 (P60881) Synaptosomal-associated protein 25 × 2 (P60881) Complexin-1 × 2 (P63041) Synaptotagmin-1 × 2 (P21707) MG MAGNESIUM ION × 2 GOL GLYCEROL × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;100 mM HEPES, pH7.4, 15-20% PEG3350, 200 mM ammonium formate Resolution 1.85 Å R-free 0.232

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 2–40; UniProt 28–66

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 191–256 Fragment:UNP residues 191-256 Vesicle-associated membrane protein 2 × 2 (P63045) Synaptosomal-associated protein 25 × 2 (P60881) Synaptosomal-associated protein 25 × 2 (P60881) Complexin-1 × 2 (P63041) Synaptotagmin-1 × 2 (P21707) MG MAGNESIUM ION × 2 GOL GLYCEROL × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;100 mM HEPES, pH7.4, 15-20% PEG3350, 200 mM ammonium formate Resolution 1.85 Å R-free 0.232

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 × 12 PDB declaration: dodecameric(12) 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 × 2 (P63045) Syntaxin-1A × 2 (P32851) Complexin-1 × 2 (P63041) Synaptotagmin-1 × 2 (P21707) MG MAGNESIUM ION × 2 GOL GLYCEROL × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;100 mM HEPES, pH7.4, 15-20% PEG3350, 200 mM ammonium formate Resolution 1.85 Å R-free 0.232

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

Complexin-1

Rattus norvegicus

UniProt P63041

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain E; UniProt 1–83 Fragment:UNP residues 1-83 Vesicle-associated membrane protein 2 × 2 (P63045) Syntaxin-1A × 2 (P32851) Synaptosomal-associated protein 25 × 2 (P60881) Synaptosomal-associated protein 25 × 2 (P60881) Synaptotagmin-1 × 2 (P21707) MG MAGNESIUM ION × 2 GOL GLYCEROL × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;100 mM HEPES, pH7.4, 15-20% PEG3350, 200 mM ammonium formate Resolution 1.85 Å R-free 0.232

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CPLX1_RAT
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–83; UniProt 1–83

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain F; UniProt 140–421 Fragment:UNP residues 140-421 Vesicle-associated membrane protein 2 × 2 (P63045) Syntaxin-1A × 2 (P32851) Synaptosomal-associated protein 25 × 2 (P60881) Synaptosomal-associated protein 25 × 2 (P60881) Complexin-1 × 2 (P63041) MG MAGNESIUM ION × 2 GOL GLYCEROL × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;100 mM HEPES, pH7.4, 15-20% PEG3350, 200 mM ammonium formate Resolution 1.85 Å R-free 0.232

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 6
Chains and sequence ranges Author chain F; PDBConstruct 1–282; UniProt 140–421

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 5w5c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5w5c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5w5c
Deposition date deposition_date2017-06-14
Structure title titleCrystal structure of the primed SNARE-Complexin-Synaptotagmin-1 C2AB complex
Keywords keywords;Prefusion primed complex, Neuronal Exocytosis, Synaptotagmin, SNARE complex, Complexin, synchronous neurotransmitter release, EXOCYTOSIS ;; EXOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.87
Radius of gyration Rg (electron density) rg_electron28.22
Forward intensity I(0) i051452900.00
Molecular weight molecular_weight53289.0 kDa
Excluded volume excluded_volume65625 ų
Envelope volume envelope_volume90236 ų
Hydration-shell volume shell_volume27713 ų
Envelope diameter envelope_diameter102.1
Shell Rg shell_rg33.99
Envelope Rg envelope_rg28.37
Shape Rg shape_rg28.31
Total Rg total_rg28.56
Total atoms total_atoms3739
Residues n_residues498
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 dmax97.7
Rg (real space) rg_real28.96
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real5.1450e+07
I(0) uncertainty (real space) i0_real_error7.3590e+05
Rg (reciprocal space) rg_reciprocal28.92
I(0) (reciprocal space) i0_reciprocal51450000.0000
Solution quality estimate total_estimate0.8773
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.402
Kurtosis Kurtosis kurtosis-0.318
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11980000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.869; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.862; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd5w5cb_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.15 — SNARE fusion complex
Family Family familyh.1.15.1 — SNARE fusion complex
Domain ID domain_idd5w5cc_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.15 — SNARE fusion complex
Family Family familyh.1.15.1 — SNARE fusion complex
Domain ID domain_idd5w5cd_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.15 — SNARE fusion complex
Family Family familyh.1.15.1 — SNARE fusion complex
Domain ID domain_idd5w5cf1
Class classb — All beta proteins
Fold Fold foldb.7 — C2 domain-like
Superfamily Superfamily superfamilyb.7.1 — C2 domain (Calcium/lipid-binding domain, CaLB)
Family Family familyb.7.1.2 — Synaptotagmin-like (S variant)
Domain ID domain_idd5w5cf2
Class classb — All beta proteins
Fold Fold foldb.7 — C2 domain-like
Superfamily Superfamily superfamilyb.7.1 — C2 domain (Calcium/lipid-binding domain, CaLB)
Family Family familyb.7.1.2 — Synaptotagmin-like (S variant)

CATH v4.4 (3 domains)

Domain ID domain_id5w5cD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily110
Domain ID domain_id5w5cF01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily150 — C2 domain
Domain ID domain_id5w5cF02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily150 — C2 domain

8. Citations (1)

9. Files and Curves (10)