1sfc

NEURONAL SYNAPTIC FUSION COMPLEX

Method: X-RAY DIFFRACTION Dmax: 157.7 Å Quality: REASONABLE

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

PROTEIN (SYNAPTOBREVIN 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–96 Fragment:PROTEOLYTICALLY PROTECTED FRAGMENT PROTEIN (SYNTAXIN 1A) × 1 (P32851) PROTEIN (SNAP-25B) × 1 (P60881) PROTEIN (SNAP-25B) × 1 (P60881) SR STRONTIUM ION × 6 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;35% MPD, 5% PEG350(MME), 25MM TRIS PH 7.0,. 70MM SRCL2, 250MM UREA, 7MM SARKOSYL Resolution 2.40 Å R-free 0.303
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–96 Fragment:PROTEOLYTICALLY PROTECTED FRAGMENT PROTEIN (SYNTAXIN 1A) × 1 (P32851) PROTEIN (SNAP-25B) × 1 (P60881) PROTEIN (SNAP-25B) × 1 (P60881) SR STRONTIUM ION × 5 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;35% MPD, 5% PEG350(MME), 25MM TRIS PH 7.0,. 70MM SRCL2, 250MM UREA, 7MM SARKOSYL Resolution 2.40 Å R-free 0.303
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain I; UniProt 1–96 Fragment:PROTEOLYTICALLY PROTECTED FRAGMENT PROTEIN (SYNTAXIN 1A) × 1 (P32851) PROTEIN (SNAP-25B) × 1 (P60881) PROTEIN (SNAP-25B) × 1 (P60881) SR STRONTIUM ION × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;35% MPD, 5% PEG350(MME), 25MM TRIS PH 7.0,. 70MM SRCL2, 250MM UREA, 7MM SARKOSYL Resolution 2.40 Å R-free 0.303

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 26 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 1–96; UniProt 1–96 Author chain E; PDBConstruct 1–96; UniProt 1–96 Author chain I; PDBConstruct 1–96; UniProt 1–96

PROTEIN (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 180–262 Fragment:PROTEOLYTICALLY PROTECTED FRAGMENT PROTEIN (SYNAPTOBREVIN 2) × 1 (P63045) PROTEIN (SNAP-25B) × 1 (P60881) PROTEIN (SNAP-25B) × 1 (P60881) SR STRONTIUM ION × 6 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;35% MPD, 5% PEG350(MME), 25MM TRIS PH 7.0,. 70MM SRCL2, 250MM UREA, 7MM SARKOSYL Resolution 2.40 Å R-free 0.303
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 180–262 Fragment:PROTEOLYTICALLY PROTECTED FRAGMENT PROTEIN (SYNAPTOBREVIN 2) × 1 (P63045) PROTEIN (SNAP-25B) × 1 (P60881) PROTEIN (SNAP-25B) × 1 (P60881) SR STRONTIUM ION × 5 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;35% MPD, 5% PEG350(MME), 25MM TRIS PH 7.0,. 70MM SRCL2, 250MM UREA, 7MM SARKOSYL Resolution 2.40 Å R-free 0.303
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain J; UniProt 180–262 Fragment:PROTEOLYTICALLY PROTECTED FRAGMENT PROTEIN (SYNAPTOBREVIN 2) × 1 (P63045) PROTEIN (SNAP-25B) × 1 (P60881) PROTEIN (SNAP-25B) × 1 (P60881) SR STRONTIUM ION × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;35% MPD, 5% PEG350(MME), 25MM TRIS PH 7.0,. 70MM SRCL2, 250MM UREA, 7MM SARKOSYL Resolution 2.40 Å R-free 0.303

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 70 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 1–83; UniProt 180–262 Author chain F; PDBConstruct 1–83; UniProt 180–262 Author chain J; PDBConstruct 1–83; UniProt 180–262

PROTEIN (SNAP-25B)

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 C; UniProt 1–83 Chain D; UniProt 120–206 Fragment:PROTEOLYTICALLY PROTECTED FRAGMENT PROTEIN (SYNAPTOBREVIN 2) × 1 (P63045) PROTEIN (SYNTAXIN 1A) × 1 (P32851) SR STRONTIUM ION × 6 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;35% MPD, 5% PEG350(MME), 25MM TRIS PH 7.0,. 70MM SRCL2, 250MM UREA, 7MM SARKOSYL Resolution 2.40 Å R-free 0.303
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 1–83 Chain H; UniProt 120–206 Fragment:PROTEOLYTICALLY PROTECTED FRAGMENT PROTEIN (SYNAPTOBREVIN 2) × 1 (P63045) PROTEIN (SYNTAXIN 1A) × 1 (P32851) SR STRONTIUM ION × 5 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;35% MPD, 5% PEG350(MME), 25MM TRIS PH 7.0,. 70MM SRCL2, 250MM UREA, 7MM SARKOSYL Resolution 2.40 Å R-free 0.303
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain K; UniProt 1–83 Chain L; UniProt 120–206 Fragment:PROTEOLYTICALLY PROTECTED FRAGMENT PROTEIN (SYNAPTOBREVIN 2) × 1 (P63045) PROTEIN (SYNTAXIN 1A) × 1 (P32851) SR STRONTIUM ION × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;35% MPD, 5% PEG350(MME), 25MM TRIS PH 7.0,. 70MM SRCL2, 250MM UREA, 7MM SARKOSYL Resolution 2.40 Å R-free 0.303

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 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNP25_RAT
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain C; PDBConstruct 1–83; UniProt 1–83 Author chain G; PDBConstruct 1–83; UniProt 1–83 Author chain K; PDBConstruct 1–83; UniProt 1–83 Author chain D; PDBConstruct 1–87; UniProt 120–206 Author chain H; PDBConstruct 1–87; UniProt 120–206 Author chain L; PDBConstruct 1–87; UniProt 120–206

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 1sfc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1sfc
Deposition date deposition_date1998-08-24
Structure title titleNEURONAL SYNAPTIC FUSION COMPLEX
Keywords keywordsMEMBRANE FUSION PROTEIN COMPLEX, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.78
Radius of gyration Rg (electron density) rg_electron40.75
Forward intensity I(0) i0186285000.00
Molecular weight molecular_weight102570.0 kDa
Excluded volume excluded_volume125160 ų
Envelope volume envelope_volume162260 ų
Hydration-shell volume shell_volume38406 ų
Envelope diameter envelope_diameter167.2
Shell Rg shell_rg38.65
Envelope Rg envelope_rg42.36
Shape Rg shape_rg40.77
Total Rg total_rg40.57
Total atoms total_atoms7086
Residues n_residues867
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 dmax157.7
Rg (real space) rg_real40.66
Rg uncertainty (real space) rg_real_error2.18
I(0) (real space) i0_real1.8630e+08
I(0) uncertainty (real space) i0_real_error3.6460e+06
Rg (reciprocal space) rg_reciprocal40.11
I(0) (reciprocal space) i0_reciprocal186200000.0000
Solution quality estimate total_estimate0.6704
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.4
Skewness Skewness skewness0.742
Kurtosis Kurtosis kurtosis0.236
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9299000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.464; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.322; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd1sfca_
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_idd1sfcb_
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_idd1sfcc_
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_idd1sfcd_
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_idd1sfce_
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_idd1sfcf_
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_idd1sfcg_
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_idd1sfch_
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_idd1sfci_
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_idd1sfcj_
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_idd1sfck_
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_idd1sfcl_
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 (12 domains)

Domain ID domain_id1sfcA00
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_id1sfcB00
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_id1sfcC00
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_id1sfcD00
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_id1sfcE00
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_id1sfcF00
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_id1sfcG00
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_id1sfcH00
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_id1sfcI00
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_id1sfcJ00
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_id1sfcK00
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_id1sfcL00
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)