6ip1

alpha-SNAP-SNARE subcomplex in the whole 20S complex

Method: ELECTRON MICROSCOPY Dmax: 110.7 Å Quality: REASONABLE

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–94 Fragment:UNP residues 1-94 Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 (P60881) Synaptosomal-associated protein 25 × 1 (P60881) Alpha-soluble NSF attachment protein × 4 (A5D7S0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 Å

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 4–97; UniProt 1–94

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 2–253 Fragment:UNP residues 2-253 Vesicle-associated membrane protein 2 × 1 (P63045) Synaptosomal-associated protein 25 × 1 (P60881) Synaptosomal-associated protein 25 × 1 (P60881) Alpha-soluble NSF attachment protein × 4 (A5D7S0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 Å

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 3–254; UniProt 2–253

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–100 Chain D; UniProt 126–206 Fragment:UNP residues 1-100 Fragment:UNP residues 126-206 Vesicle-associated membrane protein 2 × 1 (P63045) Syntaxin-1A × 1 (P32851) Alpha-soluble NSF attachment protein × 4 (A5D7S0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 Å

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 3, 4
Chains and sequence ranges Author chain C; PDBConstruct 3–102; UniProt 1–100 Author chain D; PDBConstruct 3–83; UniProt 126–206

Alpha-soluble NSF attachment protein

Bos taurus

UniProt A5D7S0

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–295 Chain F; UniProt 1–295 Chain G; UniProt 1–295 Chain H; UniProt 1–295 Not recorded Vesicle-associated membrane protein 2 × 1 (P63045) Syntaxin-1A × 1 (P32851) Synaptosomal-associated protein 25 × 1 (P60881) Synaptosomal-associated protein 25 × 1 (P60881) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A5D7S0_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 15–309; UniProt 1–295 Author chain F; PDBConstruct 15–309; UniProt 1–295 Author chain G; PDBConstruct 15–309; UniProt 1–295 Author chain H; PDBConstruct 15–309; UniProt 1–295

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 6ip1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ip1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ip1
Deposition date deposition_date2018-11-01
Structure title titlealpha-SNAP-SNARE subcomplex in the whole 20S complex
Keywords keywordsmembrane fusion, ATPase, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.02
Radius of gyration Rg (electron density) rg_electron34.27
Forward intensity I(0) i0415590000.00
Molecular weight molecular_weight160510.0 kDa
Excluded volume excluded_volume199290 ų
Envelope volume envelope_volume271450 ų
Hydration-shell volume shell_volume62657 ų
Envelope diameter envelope_diameter117.8
Shell Rg shell_rg43.01
Envelope Rg envelope_rg34.48
Shape Rg shape_rg34.28
Total Rg total_rg34.86
Total atoms total_atoms11245
Residues n_residues1420
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 dmax110.7
Rg (real space) rg_real35.14
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real4.0490e+08
I(0) uncertainty (real space) i0_real_error5.2100e+06
Rg (reciprocal space) rg_reciprocal34.95
I(0) (reciprocal space) i0_reciprocal415600000.0000
Solution quality estimate total_estimate0.7121
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.3
Skewness Skewness skewness0.254
Kurtosis Kurtosis kurtosis-0.213
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha3.3450
Highest regularization parameter α highest_alpha97730000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 0.928; Sysdev: 0.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.887

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6ip1A00
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_id6ip1D00
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)