8ub4

Cdc48-Shp1 unfolding native substrate, consensus structure

Method: ELECTRON MICROSCOPY Dmax: 144.0 Å Quality: GOOD

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

Cell division control protein 48

OrganismNot specified

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 × 10 PDB declaration: decameric(10) 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 Substrate × 1 UBX domain-containing protein 1 × 3 (P34223) 08T [[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-tris(fluoranyl)beryllium × 8 MG MAGNESIUM ION × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 1–835; UniProt 1–835 Author chain B; PDBConstruct 1–835; UniProt 1–835 Author chain C; PDBConstruct 1–835; UniProt 1–835 Author chain D; PDBConstruct 1–835; UniProt 1–835 Author chain E; PDBConstruct 1–835; UniProt 1–835 Author chain F; PDBConstruct 1–835; UniProt 1–835

UBX domain-containing protein 1

OrganismNot specified

UniProt P34223

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain H; UniProt 1–423 Chain I; UniProt 1–423 Chain J; UniProt 1–423 Not recorded Cell division control protein 48 × 6 (P25694) Substrate × 1 08T [[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-tris(fluoranyl)beryllium × 8 MG MAGNESIUM ION × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBX1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–423; UniProt 1–423 Author chain I; PDBConstruct 1–423; UniProt 1–423 Author chain J; PDBConstruct 1–423; UniProt 1–423

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 8ub4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ub4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ub4
Deposition date deposition_date2023-09-22
Structure title titleCdc48-Shp1 unfolding native substrate, consensus structure
Keywords keywordsunfoldase, AAA ATPase, p97, CHAPERONE, Cdc48; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.07
Radius of gyration Rg (electron density) rg_electron45.22
Forward intensity I(0) i01721780000.00
Molecular weight molecular_weight325460.0 kDa
Excluded volume excluded_volume397730 ų
Envelope volume envelope_volume602540 ų
Hydration-shell volume shell_volume104170 ų
Envelope diameter envelope_diameter147.9
Shell Rg shell_rg54.59
Envelope Rg envelope_rg44.76
Shape Rg shape_rg44.95
Total Rg total_rg46.40
Total atoms total_atoms43895
Residues n_residues3274
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 dmax144.0
Rg (real space) rg_real45.74
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.7220e+09
I(0) uncertainty (real space) i0_real_error2.7220e+07
Rg (reciprocal space) rg_reciprocal46.07
I(0) (reciprocal space) i0_reciprocal1722000000.0000
Solution quality estimate total_estimate0.8865
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.3
Skewness Skewness skewness0.113
Kurtosis Kurtosis kurtosis-0.482
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha249600000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.950; Smooth: 0.897

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)