6mdp

The D1 and D2 domain rings of NSF engaging the SNAP-25 N-terminus within the 20S supercomplex (focused refinement on D1/D2 rings, class 2)

Method: ELECTRON MICROSCOPY Dmax: 143.7 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 × 7 PDB declaration: heptameric(7) 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) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 3.5 seconds before plunging. Resolution 3.80 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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain H; UniProt 1–204 Not recorded Vesicle-fusing ATPase × 6 (P18708) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 3.5 seconds before plunging. Resolution 3.80 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

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 6mdp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6mdp
Deposition date deposition_date2018-09-04
Structure title titleThe D1 and D2 domain rings of NSF engaging the SNAP-25 N-terminus within the 20S supercomplex (focused refinement on D1/D2 rings, 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_guinier46.34
Radius of gyration Rg (electron density) rg_electron45.60
Forward intensity I(0) i01485690000.00
Molecular weight molecular_weight320490.0 kDa
Excluded volume excluded_volume402070 ų
Envelope volume envelope_volume569170 ų
Hydration-shell volume shell_volume98371 ų
Envelope diameter envelope_diameter145.3
Shell Rg shell_rg54.62
Envelope Rg envelope_rg44.82
Shape Rg shape_rg45.63
Total Rg total_rg45.81
Total atoms total_atoms45342
Residues n_residues2832
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 dmax143.7
Rg (real space) rg_real45.98
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.4860e+09
I(0) uncertainty (real space) i0_real_error2.3800e+07
Rg (reciprocal space) rg_reciprocal46.34
I(0) (reciprocal space) i0_reciprocal1486000000.0000
Solution quality estimate total_estimate0.8904
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.2
Skewness Skewness skewness0.047
Kurtosis Kurtosis kurtosis-0.532
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha145900000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.899

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6mdpF01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6mdpF02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60

8. Citations (1)

9. Files and Curves (10)