8dat

Saccharomyces cerevisiae Ufd1/Npl4/Cdc48 complex bound to three ubiquitin moieties in presence of SUMO-ubiquitin(K48polyUb)-mEOS and ATP, state 1 (intB)

Method: ELECTRON MICROSCOPY Dmax: 178.9 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 × 11 PDB declaration: undecameric(11) 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) Ubiquitin × 3 (P0CG63) ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 7 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 3.80 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.

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 × 11 PDB declaration: undecameric(11) 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) Ubiquitin × 3 (P0CG63) ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 7 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 3.80 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.

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 × 11 PDB declaration: undecameric(11) 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) Ubiquitin × 3 (P0CG63) ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 7 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 3.80 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.

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

Ubiquitin

Saccharomyces cerevisiae

UniProt P0CG63

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 1–76 Chain K; UniProt 1–76 Chain L; UniProt 1–76 Not recorded Cell division control protein 48 × 6 (P25694) Nuclear protein localization protein 4 × 1 (P33755) Ubiquitin fusion degradation protein 1 × 1 (P53044) ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 7 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 3.80 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBI4P_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain J; PDBConstruct 1–76; UniProt 1–76 Author chain K; PDBConstruct 1–76; UniProt 1–76 Author chain L; PDBConstruct 1–76; UniProt 1–76

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 8dat

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8dat
Deposition date deposition_date2022-06-14
Structure title titleSaccharomyces cerevisiae Ufd1/Npl4/Cdc48 complex bound to three ubiquitin moieties in presence of SUMO-ubiquitin(K48polyUb)-mEOS and ATP, state 1 (intB)
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_guinier54.64
Radius of gyration Rg (electron density) rg_electron54.49
Forward intensity I(0) i03565730000.00
Molecular weight molecular_weight493660.0 kDa
Excluded volume excluded_volume615150 ų
Envelope volume envelope_volume905650 ų
Hydration-shell volume shell_volume132600 ų
Envelope diameter envelope_diameter186.0
Shell Rg shell_rg62.12
Envelope Rg envelope_rg53.91
Shape Rg shape_rg54.53
Total Rg total_rg54.54
Total atoms total_atoms34635
Residues n_residues4388
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 dmax178.9
Rg (real space) rg_real54.47
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real3.5660e+09
I(0) uncertainty (real space) i0_real_error6.5380e+07
Rg (reciprocal space) rg_reciprocal54.78
I(0) (reciprocal space) i0_reciprocal3567000000.0000
Solution quality estimate total_estimate0.8617
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.8
Skewness Skewness skewness0.265
Kurtosis Kurtosis kurtosis-0.251
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha623500000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.730

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8datJ01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id8datK01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id8datL01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)