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
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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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 11 Nuclear protein localization protein 4 × 1 (P33755) Ubiquitin fusion degradation protein 1 × 1 (P53044) Ubiquitin × 3 (P0CG63) ADENOSINE-5'-TRIPHOSPHATE × 5 ADENOSINE-5'-DIPHOSPHATE × 7 ZINC ION × 2 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 11 Cell division control protein 48 × 6 (P25694) Ubiquitin fusion degradation protein 1 × 1 (P53044) Ubiquitin × 3 (P0CG63) ADENOSINE-5'-TRIPHOSPHATE × 5 ADENOSINE-5'-DIPHOSPHATE × 7 ZINC ION × 2 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 11 Cell division control protein 48 × 6 (P25694) Nuclear protein localization protein 4 × 1 (P33755) Ubiquitin × 3 (P0CG63) ADENOSINE-5'-TRIPHOSPHATE × 5 ADENOSINE-5'-DIPHOSPHATE × 7 ZINC ION × 2 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 11 Cell division control protein 48 × 6 (P25694) Nuclear protein localization protein 4 × 1 (P33755) Ubiquitin fusion degradation protein 1 × 1 (P53044) ADENOSINE-5'-TRIPHOSPHATE × 5 ADENOSINE-5'-DIPHOSPHATE × 7 ZINC ION × 2 Consistent with protein count

Other States of the Same Protein in the Database

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.

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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
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8dat__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8dat__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8dat__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)54.64 Å
Rg (electron density)54.49 Å
Total Rg54.54 Å
Atom count34635
Residues4388
Excluded volume615150 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8dat__assembly_1__model_1 undecameric (11) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (7)

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6. 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
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7. Citations (1)