3rk3

Truncated SNARE complex with complexin

Method: X-RAY DIFFRACTION Dmax: 109.0 Å Quality: REASONABLE

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

Vamp2

Homo sapiens

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 28–60 Fragment:UNP residues 28-60 Syntaxin 1a × 1 (P32851) SNAP25 × 1 (P60880) SNAP25 × 1 (P60880) Complexin-1 × 1 (O14810) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;294 K;13-15% polyethyleneglycol (PEG) 5000MME, 0.2 M ammonium sulfate, 0.01 M EDTA, 0.1 M Tris pH 7.5, VAPOR DIFFUSION, temperature 294K Resolution 3.50 Å R-free 0.316

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 1
Chains and sequence ranges Author chain A; PDBConstruct 5–37; UniProt 28–60

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 191–253 Fragment:UNP residues 191-253 Vamp2 × 1 (P63027) SNAP25 × 1 (P60880) SNAP25 × 1 (P60880) Complexin-1 × 1 (O14810) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;294 K;13-15% polyethyleneglycol (PEG) 5000MME, 0.2 M ammonium sulfate, 0.01 M EDTA, 0.1 M Tris pH 7.5, VAPOR DIFFUSION, temperature 294K Resolution 3.50 Å R-free 0.316

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 3–65; UniProt 191–253

SNAP25

Homo sapiens

UniProt P60880

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 7–82 Chain D; UniProt 141–203 Fragment:UNP residues 7-82 Fragment:UNP residues 141-203 Vamp2 × 1 (P63027) Syntaxin 1a × 1 (P32851) Complexin-1 × 1 (O14810) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;294 K;13-15% polyethyleneglycol (PEG) 5000MME, 0.2 M ammonium sulfate, 0.01 M EDTA, 0.1 M Tris pH 7.5, VAPOR DIFFUSION, temperature 294K Resolution 3.50 Å R-free 0.316

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.

10 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNP25_HUMAN
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain C; PDBConstruct 5–80; UniProt 7–82 Author chain D; PDBConstruct 3–65; UniProt 141–203

Complexin-1

Homo sapiens

UniProt O14810

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 26–83 Fragment:UNP residues 26-83 Vamp2 × 1 (P63027) Syntaxin 1a × 1 (P32851) SNAP25 × 1 (P60880) SNAP25 × 1 (P60880) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;294 K;13-15% polyethyleneglycol (PEG) 5000MME, 0.2 M ammonium sulfate, 0.01 M EDTA, 0.1 M Tris pH 7.5, VAPOR DIFFUSION, temperature 294K Resolution 3.50 Å R-free 0.316

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.

1 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CPLX1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 6–63; UniProt 26–83

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 3rk3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3rk3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3rk3
Deposition date deposition_date2011-04-17
Structure title titleTruncated SNARE complex with complexin
Keywords keywordsSNARE proteins, membrane fusion, MEMBRANE PROTEIN-EXOCYTOSIS-TRANSPORT PROTEIN complex, MEMBRANE PROTEIN-EXOCYTOSIS complex; MEMBRANE PROTEIN/EXOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.36
Radius of gyration Rg (electron density) rg_electron28.75
Forward intensity I(0) i020622200.00
Molecular weight molecular_weight31792.0 kDa
Excluded volume excluded_volume38639 ų
Envelope volume envelope_volume54491 ų
Hydration-shell volume shell_volume18634 ų
Envelope diameter envelope_diameter115.6
Shell Rg shell_rg30.51
Envelope Rg envelope_rg30.42
Shape Rg shape_rg28.76
Total Rg total_rg28.92
Total atoms total_atoms2215
Residues n_residues276
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 dmax109.0
Rg (real space) rg_real29.04
Rg uncertainty (real space) rg_real_error1.57
I(0) (real space) i0_real2.0620e+07
I(0) uncertainty (real space) i0_real_error3.4120e+05
Rg (reciprocal space) rg_reciprocal28.83
I(0) (reciprocal space) i0_reciprocal20620000.0000
Solution quality estimate total_estimate0.7192
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.714
Kurtosis Kurtosis kurtosis-0.021
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2755000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.411; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.133; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3rk3B00
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_id3rk3C00
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_id3rk3D00
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_id3rk3E00
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 superfamily580 — Single Helix bin

8. Citations (1)

9. Files and Curves (10)