1jth

Crystal structure and biophysical properties of a complex between the N-terminal region of SNAP25 and the SNARE region of syntaxin 1a

Method: X-RAY DIFFRACTION Dmax: 104.1 Å Quality: REASONABLE

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

SNAP25

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–82 Chain C; UniProt 1–82 Fragment:N-terminal SNARE motif syntaxin 1a × 2 (P32851) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;294 K;ammonium sulfate, MES, pH 6.5, VAPOR DIFFUSION, temperature 294K Resolution 2.00 Å R-free 0.289

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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–82; UniProt 1–82 Author chain C; PDBConstruct 1–82; UniProt 1–82

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 191–267 Chain D; UniProt 191–267 Fragment:H3, SNARE motif SNAP25 × 2 (P60881) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;294 K;ammonium sulfate, MES, pH 6.5, VAPOR DIFFUSION, temperature 294K Resolution 2.00 Å R-free 0.289

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 1–77; UniProt 191–267 Author chain D; PDBConstruct 1–77; UniProt 191–267

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 1jth

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jth
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jth
Deposition date deposition_date2001-08-21
Structure title titleCrystal structure and biophysical properties of a complex between the N-terminal region of SNAP25 and the SNARE region of syntaxin 1a
Keywords keywordscoiled-coil, polar layer, ENDOCYTOSIS-EXOCYTOSIS COMPLEX; ENDOCYTOSIS/EXOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.08
Radius of gyration Rg (electron density) rg_electron27.68
Forward intensity I(0) i016277800.00
Molecular weight molecular_weight28820.0 kDa
Excluded volume excluded_volume35258 ų
Envelope volume envelope_volume45263 ų
Hydration-shell volume shell_volume16408 ų
Envelope diameter envelope_diameter109.2
Shell Rg shell_rg29.50
Envelope Rg envelope_rg28.89
Shape Rg shape_rg27.71
Total Rg total_rg27.77
Total atoms total_atoms2005
Residues n_residues249
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 dmax104.1
Rg (real space) rg_real27.78
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real1.6280e+07
I(0) uncertainty (real space) i0_real_error2.8780e+05
Rg (reciprocal space) rg_reciprocal27.56
I(0) (reciprocal space) i0_reciprocal16280000.0000
Solution quality estimate total_estimate0.6554
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.737
Kurtosis Kurtosis kurtosis-0.144
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6524000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.169; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.017; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1jtha_
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_idd1jthb_
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_idd1jthc_
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_idd1jthd_
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

CATH v4.4 (4 domains)

Domain ID domain_id1jthA00
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_id1jthB00
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_id1jthC00
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_id1jthD00
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

8. Citations (1)

9. Files and Curves (10)