8i79

Cryo-EM structure of KCTD7 in complex with Cullin3

Method: ELECTRON MICROSCOPY Dmax: 174.2 Å Quality: GOOD

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

BTB/POZ domain-containing protein KCTD7

Mus musculus

UniProt Q8BJK1

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 1–289 Chain D; UniProt 1–289 Chain F; UniProt 1–289 Chain G; UniProt 1–289 Chain I; UniProt 1–289 Mutation:H126Y Cullin-3 × 5 (Q13618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

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

View Construct and Data Evidence
UniProt name KCTD7_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–297; UniProt 1–289 Author chain D; PDBConstruct 9–297; UniProt 1–289 Author chain F; PDBConstruct 9–297; UniProt 1–289 Author chain G; PDBConstruct 9–297; UniProt 1–289 Author chain I; PDBConstruct 9–297; UniProt 1–289

Cullin-3

Homo sapiens

UniProt Q13618

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 B; UniProt 22–388 Chain C; UniProt 22–388 Chain E; UniProt 22–388 Chain H; UniProt 22–388 Chain J; UniProt 22–388 Mutation:I342R, L346D BTB/POZ domain-containing protein KCTD7 × 5 (Q8BJK1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

29 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 10–376; UniProt 22–388 Author chain C; PDBConstruct 10–376; UniProt 22–388 Author chain E; PDBConstruct 10–376; UniProt 22–388 Author chain H; PDBConstruct 10–376; UniProt 22–388 Author chain J; PDBConstruct 10–376; UniProt 22–388

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 8i79

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8i79
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8i79
Deposition date deposition_date2023-01-31
Structure title titleCryo-EM structure of KCTD7 in complex with Cullin3
Keywords keywordsCUL3, ubiquitination, E3 ligase, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.43
Radius of gyration Rg (electron density) rg_electron47.10
Forward intensity I(0) i0816122000.00
Molecular weight molecular_weight230420.0 kDa
Excluded volume excluded_volume285610 ų
Envelope volume envelope_volume432750 ų
Hydration-shell volume shell_volume76905 ų
Envelope diameter envelope_diameter175.4
Shell Rg shell_rg50.62
Envelope Rg envelope_rg47.71
Shape Rg shape_rg47.20
Total Rg total_rg46.88
Total atoms total_atoms16293
Residues n_residues2198
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 dmax174.2
Rg (real space) rg_real48.41
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real8.1610e+08
I(0) uncertainty (real space) i0_real_error1.7410e+07
Rg (reciprocal space) rg_reciprocal48.43
I(0) (reciprocal space) i0_reciprocal816100000.0000
Solution quality estimate total_estimate0.8347
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.1
Skewness Skewness skewness0.366
Kurtosis Kurtosis kurtosis-0.155
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46960000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.628; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)