6mdn

The 20S supercomplex engaging the SNAP-25 N-terminus (class 2)

Method: ELECTRON MICROSCOPY Dmax: 209.6 Å Quality: GOOD

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

Vesicle-fusing ATPase

Cricetulus griseus

UniProt P18708

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain A; UniProt 1–723 Chain B; UniProt 1–723 Chain C; UniProt 1–723 Chain D; UniProt 1–723 Chain E; UniProt 1–723 Chain F; UniProt 1–723 Not recorded Synaptosomal-associated protein 25 × 1 (P60881) Syntaxin-1A × 1 (P32851) Vesicle-associated membrane protein 2 × 1 (P63045) Alpha-soluble NSF attachment protein × 2 (P54921) ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 3.5 seconds before plunging. Resolution 4.40 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.

41 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NSF_CRIGR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 25–747; UniProt 1–723 Author chain B; PDBConstruct 25–747; UniProt 1–723 Author chain C; PDBConstruct 25–747; UniProt 1–723 Author chain D; PDBConstruct 25–747; UniProt 1–723 Author chain E; PDBConstruct 25–747; UniProt 1–723 Author chain F; PDBConstruct 25–747; UniProt 1–723

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain H; UniProt 1–204 Not recorded Vesicle-fusing ATPase × 6 (P18708) Syntaxin-1A × 1 (P32851) Vesicle-associated membrane protein 2 × 1 (P63045) Alpha-soluble NSF attachment protein × 2 (P54921) ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 3.5 seconds before plunging. Resolution 4.40 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 P60881-2
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 4–207; UniProt 1–204

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain I; UniProt 1–256 Not recorded Vesicle-fusing ATPase × 6 (P18708) Synaptosomal-associated protein 25 × 1 (P60881) Vesicle-associated membrane protein 2 × 1 (P63045) Alpha-soluble NSF attachment protein × 2 (P54921) ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 3.5 seconds before plunging. Resolution 4.40 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 3
Chains and sequence ranges Author chain I; PDBConstruct 1–256; UniProt 1–256

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain J; UniProt 1–72 Not recorded Vesicle-fusing ATPase × 6 (P18708) Synaptosomal-associated protein 25 × 1 (P60881) Syntaxin-1A × 1 (P32851) Alpha-soluble NSF attachment protein × 2 (P54921) ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 3.5 seconds before plunging. Resolution 4.40 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 4
Chains and sequence ranges Author chain J; PDBConstruct 29–100; UniProt 1–72

Alpha-soluble NSF attachment protein

Rattus norvegicus

UniProt P54921

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain K; UniProt 1–278 Chain L; UniProt 1–278 Not recorded Vesicle-fusing ATPase × 6 (P18708) Synaptosomal-associated protein 25 × 1 (P60881) Syntaxin-1A × 1 (P32851) Vesicle-associated membrane protein 2 × 1 (P63045) ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 3.5 seconds before plunging. Resolution 4.40 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.

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

View Construct and Data Evidence
UniProt name SNAA_RAT
Isoform
PDB entities 5
Chains and sequence ranges Author chain K; PDBConstruct 19–296; UniProt 1–278 Author chain L; PDBConstruct 19–296; UniProt 1–278

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 6mdn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6mdn
Deposition date deposition_date2018-09-04
Structure title titleThe 20S supercomplex engaging the SNAP-25 N-terminus (class 2)
Keywords keywordsSNARE, NSF, SNAP, ATPase, AAA, disassembly, synapse, membrane fusion, exocytosis, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.26
Radius of gyration Rg (electron density) rg_electron62.31
Forward intensity I(0) i03854170000.00
Molecular weight molecular_weight519740.0 kDa
Excluded volume excluded_volume650120 ų
Envelope volume envelope_volume1017600 ų
Hydration-shell volume shell_volume136770 ų
Envelope diameter envelope_diameter221.9
Shell Rg shell_rg64.80
Envelope Rg envelope_rg60.49
Shape Rg shape_rg62.33
Total Rg total_rg62.31
Total atoms total_atoms73042
Residues n_residues4632
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 dmax209.6
Rg (real space) rg_real62.34
Rg uncertainty (real space) rg_real_error3.04
I(0) (real space) i0_real3.8540e+09
I(0) uncertainty (real space) i0_real_error9.2360e+07
Rg (reciprocal space) rg_reciprocal62.18
I(0) (reciprocal space) i0_reciprocal3853000000.0000
Solution quality estimate total_estimate0.8450
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary67.1
Skewness Skewness skewness0.416
Kurtosis Kurtosis kurtosis-0.184
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha268700000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.821; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.539

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)