9o04

CryoEM structure of the FBXO42-CCDC6-PP2Ac degradasome

Method: ELECTRON MICROSCOPY Dmax: 189.9 Å Quality: GOOD

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

Coiled-coil domain-containing protein 6

Homo sapiens

UniProt Q16204

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain A; UniProt 1–474 Chain B; UniProt 1–474 Not recorded F-box only protein 42 × 2 (Q6P3S6) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 8 (P67775) SKP1 × 2 MN MANGANESE (II) ION × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 200 mM NaCl, 1 mM TCEP pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 CCDC6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 17–490; UniProt 1–474 Author chain B; PDBConstruct 17–490; UniProt 1–474

F-box only protein 42

Homo sapiens

UniProt Q6P3S6

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain C; UniProt 44–717 Chain G; UniProt 44–717 Not recorded Coiled-coil domain-containing protein 6 × 2 (Q16204) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 8 (P67775) SKP1 × 2 MN MANGANESE (II) ION × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 200 mM NaCl, 1 mM TCEP pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name FBX42_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 18–691; UniProt 44–717 Author chain G; PDBConstruct 18–691; UniProt 44–717

Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform

Homo sapiens

UniProt P67775

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain D; UniProt 1–309 Chain E; UniProt 1–309 Chain I; UniProt 1–309 Chain J; UniProt 1–309 Chain K; UniProt 1–309 Chain L; UniProt 1–309 Chain M; UniProt 1–309 Chain N; UniProt 1–309 Non-standard monomer:Yes (specific site not provided by mmCIF) Coiled-coil domain-containing protein 6 × 2 (Q16204) F-box only protein 42 × 2 (Q6P3S6) SKP1 × 2 MN MANGANESE (II) ION × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 200 mM NaCl, 1 mM TCEP pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

49 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP2AA_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 28–336; UniProt 1–309 Author chain E; PDBConstruct 28–336; UniProt 1–309 Author chain I; PDBConstruct 28–336; UniProt 1–309 Author chain J; PDBConstruct 28–336; UniProt 1–309 Author chain K; PDBConstruct 28–336; UniProt 1–309 Author chain L; PDBConstruct 28–336; UniProt 1–309 Author chain M; PDBConstruct 28–336; UniProt 1–309 Author chain N; PDBConstruct 28–336; UniProt 1–309

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 9o04

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9o04
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9o04
Deposition date deposition_date2025-04-02
Structure title titleCryoEM structure of the FBXO42-CCDC6-PP2Ac degradasome
Keywords keywordsE3 ligase, phosphatase, scaffolding, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.84
Radius of gyration Rg (electron density) rg_electron63.28
Forward intensity I(0) i02511190000.00
Molecular weight molecular_weight417280.0 kDa
Excluded volume excluded_volume519940 ų
Envelope volume envelope_volume800080 ų
Hydration-shell volume shell_volume109060 ų
Envelope diameter envelope_diameter208.4
Shell Rg shell_rg59.29
Envelope Rg envelope_rg62.23
Shape Rg shape_rg63.26
Total Rg total_rg63.27
Total atoms total_atoms29334
Residues n_residues3634
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 dmax189.9
Rg (real space) rg_real63.04
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real2.5110e+09
I(0) uncertainty (real space) i0_real_error4.6380e+07
Rg (reciprocal space) rg_reciprocal62.63
I(0) (reciprocal space) i0_reciprocal2509000000.0000
Solution quality estimate total_estimate0.8439
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary68.4
Skewness Skewness skewness0.377
Kurtosis Kurtosis kurtosis-0.340
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha75690000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.082

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)