8dar

Saccharomyces cerevisiae Ufd1/Npl4/Cdc48 complex unbound but in the presence of SUMO-ubiquitin(K48polyUb)-mEOS and ATP

Method: ELECTRON MICROSCOPY Dmax: 156.3 Å Quality: GOOD

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

Cell division control protein 48

Saccharomyces cerevisiae

UniProt P25694

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 1–835 Chain B; UniProt 1–835 Chain C; UniProt 1–835 Chain D; UniProt 1–835 Chain E; UniProt 1–835 Chain F; UniProt 1–835 Not recorded Nuclear protein localization protein 4 × 1 (P33755) Ubiquitin fusion degradation protein 1 × 1 (P53044) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8.0, 150 mM NaCl, 0.1 mM TCEP, 1 mM MgCl2, 5 mM ATP. Added 0.05% CHAPSO before vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;8 s wait, 4 s blot before plunging Resolution 3.00 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 CDC48_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–838; UniProt 1–835 Author chain B; PDBConstruct 4–838; UniProt 1–835 Author chain C; PDBConstruct 4–838; UniProt 1–835 Author chain D; PDBConstruct 4–838; UniProt 1–835 Author chain E; PDBConstruct 4–838; UniProt 1–835 Author chain F; PDBConstruct 4–838; UniProt 1–835

Nuclear protein localization protein 4

Saccharomyces cerevisiae

UniProt P33755

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 G; UniProt 1–580 Not recorded Cell division control protein 48 × 6 (P25694) Ubiquitin fusion degradation protein 1 × 1 (P53044) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8.0, 150 mM NaCl, 0.1 mM TCEP, 1 mM MgCl2, 5 mM ATP. Added 0.05% CHAPSO before vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;8 s wait, 4 s blot before plunging Resolution 3.00 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.

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

View Construct and Data Evidence
UniProt name NPL4_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 4–583; UniProt 1–580

Ubiquitin fusion degradation protein 1

Saccharomyces cerevisiae

UniProt P53044

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 H; UniProt 1–361 Not recorded Cell division control protein 48 × 6 (P25694) Nuclear protein localization protein 4 × 1 (P33755) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8.0, 150 mM NaCl, 0.1 mM TCEP, 1 mM MgCl2, 5 mM ATP. Added 0.05% CHAPSO before vitrification. cryo-EM vitrification conditions:Cryogen ETHANE;8 s wait, 4 s blot before plunging Resolution 3.00 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UFD1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 3–363; UniProt 1–361

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 8dar

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8dar
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8dar
Deposition date deposition_date2022-06-14
Structure title titleSaccharomyces cerevisiae Ufd1/Npl4/Cdc48 complex unbound but in the presence of SUMO-ubiquitin(K48polyUb)-mEOS and ATP
Keywords keywordsATPASE, ATPASE COMPLEX, UBIQUITIN, SUMO, SMT3, QUALITY CONTROL, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.01
Radius of gyration Rg (electron density) rg_electron49.67
Forward intensity I(0) i02742540000.00
Molecular weight molecular_weight430040.0 kDa
Excluded volume excluded_volume535230 ų
Envelope volume envelope_volume758560 ų
Hydration-shell volume shell_volume119840 ų
Envelope diameter envelope_diameter170.1
Shell Rg shell_rg59.38
Envelope Rg envelope_rg48.96
Shape Rg shape_rg49.72
Total Rg total_rg49.77
Total atoms total_atoms30157
Residues n_residues3827
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 dmax156.3
Rg (real space) rg_real49.78
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real2.7430e+09
I(0) uncertainty (real space) i0_real_error5.2830e+07
Rg (reciprocal space) rg_reciprocal50.19
I(0) (reciprocal space) i0_reciprocal2744000000.0000
Solution quality estimate total_estimate0.8844
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.5
Skewness Skewness skewness0.114
Kurtosis Kurtosis kurtosis-0.422
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha743700000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.860

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)