9nlz

Y20S (Sec18-Sec17-Sec9-Sso1-Snc1) EDTA - Class 8

Method: ELECTRON MICROSCOPY Dmax: 226.3 Å Quality: GOOD

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

Vesicular-fusion protein SEC18

Saccharomyces cerevisiae

UniProt P18759

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–758 Chain B; UniProt 1–758 Chain C; UniProt 1–758 Chain D; UniProt 1–758 Chain E; UniProt 1–758 Chain F; UniProt 1–758 Not recorded Alpha-soluble NSF attachment protein × 3 (P32602) Synaptobrevin homolog 1 × 1 (P31109) Protein SSO1 × 1 (P32867) Protein transport protein SEC9 × 1 (P40357) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.13 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.

14 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEC18_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–761; UniProt 1–758 Author chain B; PDBConstruct 4–761; UniProt 1–758 Author chain C; PDBConstruct 4–761; UniProt 1–758 Author chain D; PDBConstruct 4–761; UniProt 1–758 Author chain E; PDBConstruct 4–761; UniProt 1–758 Author chain F; PDBConstruct 4–761; UniProt 1–758

Alpha-soluble NSF attachment protein

Saccharomyces cerevisiae

UniProt P32602

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain G; UniProt 1–292 Chain H; UniProt 1–292 Chain I; UniProt 1–292 Not recorded Vesicular-fusion protein SEC18 × 6 (P18759) Synaptobrevin homolog 1 × 1 (P31109) Protein SSO1 × 1 (P32867) Protein transport protein SEC9 × 1 (P40357) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.13 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.

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

View Construct and Data Evidence
UniProt name SEC17_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 2–293; UniProt 1–292 Author chain H; PDBConstruct 2–293; UniProt 1–292 Author chain I; PDBConstruct 2–293; UniProt 1–292

Synaptobrevin homolog 1

Saccharomyces cerevisiae

UniProt P31109

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain J; UniProt 1–93 Not recorded Vesicular-fusion protein SEC18 × 6 (P18759) Alpha-soluble NSF attachment protein × 3 (P32602) Protein SSO1 × 1 (P32867) Protein transport protein SEC9 × 1 (P40357) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.13 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.

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

View Construct and Data Evidence
UniProt name SNC1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 5–97; UniProt 1–93

Protein SSO1

Saccharomyces cerevisiae

UniProt P32867

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain K; UniProt 1–265 Not recorded Vesicular-fusion protein SEC18 × 6 (P18759) Alpha-soluble NSF attachment protein × 3 (P32602) Synaptobrevin homolog 1 × 1 (P31109) Protein transport protein SEC9 × 1 (P40357) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.13 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.

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SSO1_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 5–269; UniProt 1–265

Protein transport protein SEC9

Saccharomyces cerevisiae

UniProt P40357

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain L; UniProt 433–650 Not recorded Vesicular-fusion protein SEC18 × 6 (P18759) Alpha-soluble NSF attachment protein × 3 (P32602) Synaptobrevin homolog 1 × 1 (P31109) Protein SSO1 × 1 (P32867) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.13 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.

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

View Construct and Data Evidence
UniProt name SEC9_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain L; PDBConstruct 5–222; UniProt 433–650

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 9nlz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9nlz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9nlz
Deposition date deposition_date2025-03-03
最后修订 last_revision2025-10-01
Structure title titleY20S (Sec18-Sec17-Sec9-Sso1-Snc1) EDTA - Class 8
Keywords keywordsSNARE, NSF, Sec18, AAA+, TRANSLOCASE; TRANSLOCASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.87
Radius of gyration Rg (electron density) rg_electron65.38
Forward intensity I(0) i04934360000.00
Molecular weight molecular_weight586990.0 kDa
Excluded volume excluded_volume732840 ų
Envelope volume envelope_volume1222100 ų
Hydration-shell volume shell_volume154450 ų
Envelope diameter envelope_diameter228.9
Shell Rg shell_rg69.93
Envelope Rg envelope_rg62.46
Shape Rg shape_rg65.38
Total Rg total_rg65.48
Total atoms total_atoms82446
Residues n_residues5221
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 dmax226.3
Rg (real space) rg_real65.67
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real4.9340e+09
I(0) uncertainty (real space) i0_real_error9.1620e+07
Rg (reciprocal space) rg_reciprocal66.01
I(0) (reciprocal space) i0_reciprocal4937000000.0000
Solution quality estimate total_estimate0.8565
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.5
Skewness Skewness skewness0.276
Kurtosis Kurtosis kurtosis-0.294
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha340600000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.802; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.750

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)