9qx0

Cryo-EM structure of the human UBR4/KCMF1/CALM1 complex (C-term focused refinement)

Method: ELECTRON MICROSCOPY Dmax: 185.8 Å Quality: GOOD

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

E3 ubiquitin-protein ligase KCMF1

Homo sapiens

UniProt Q9P0J7

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–381 Chain D; UniProt 1–381 Not recorded Calmodulin-1 × 1 (P0DP23) E3 ubiquitin-protein ligase UBR4 × 2 (Q5T4S7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCMF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–381; UniProt 1–381 Author chain D; PDBConstruct 1–381; UniProt 1–381

Calmodulin-1

Homo sapiens

UniProt P0DP23

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 1–149 Not recorded E3 ubiquitin-protein ligase KCMF1 × 2 (Q9P0J7) E3 ubiquitin-protein ligase UBR4 × 2 (Q5T4S7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

213 other PDB entries and 279 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 10–158; UniProt 1–149

E3 ubiquitin-protein ligase UBR4

Homo sapiens

UniProt Q5T4S7

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–5183 Chain B; UniProt 1–5183 Not recorded E3 ubiquitin-protein ligase KCMF1 × 2 (Q9P0J7) Calmodulin-1 × 1 (P0DP23) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBR4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–5183; UniProt 1–5183 Author chain B; PDBConstruct 1–5183; UniProt 1–5183

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 9qx0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qx0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9qx0
Deposition date deposition_date2025-04-15
Structure title titleCryo-EM structure of the human UBR4/KCMF1/CALM1 complex (C-term focused refinement)
Keywords keywordsUbiquitin ligase, protein quality control, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.92
Radius of gyration Rg (electron density) rg_electron54.29
Forward intensity I(0) i0557253000.00
Molecular weight molecular_weight160190.0 kDa
Excluded volume excluded_volume184920 ų
Envelope volume envelope_volume399750 ų
Hydration-shell volume shell_volume66023 ų
Envelope diameter envelope_diameter195.1
Shell Rg shell_rg51.29
Envelope Rg envelope_rg53.32
Shape Rg shape_rg54.29
Total Rg total_rg54.17
Total atoms total_atoms11445
Residues n_residues2306
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 dmax185.8
Rg (real space) rg_real54.13
Rg uncertainty (real space) rg_real_error2.42
I(0) (real space) i0_real5.5730e+08
I(0) uncertainty (real space) i0_real_error1.1930e+07
Rg (reciprocal space) rg_reciprocal53.74
I(0) (reciprocal space) i0_reciprocal556900000.0000
Solution quality estimate total_estimate0.8591
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.1
Skewness Skewness skewness0.466
Kurtosis Kurtosis kurtosis0.006
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41790000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.596

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)