9qwu

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

Method: ELECTRON MICROSCOPY Dmax: 145.9 Å Quality: GOOD

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

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–149 Chain F; UniProt 1–149 Not recorded E3 ubiquitin-protein ligase UBR4 × 2 (Q5T4S7) E3 ubiquitin-protein ligase KCMF1 × 2 (Q9P0J7) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 1
Chains and sequence ranges Author chain E; PDBConstruct 10–158; UniProt 1–149 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–5183 Chain B; UniProt 1–5183 Not recorded Calmodulin-1 × 2 (P0DP23) E3 ubiquitin-protein ligase KCMF1 × 2 (Q9P0J7) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–5183; UniProt 1–5183 Author chain B; PDBConstruct 1–5183; UniProt 1–5183

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–381 Chain D; UniProt 1–381 Not recorded Calmodulin-1 × 2 (P0DP23) E3 ubiquitin-protein ligase UBR4 × 2 (Q5T4S7) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–381; UniProt 1–381 Author chain D; PDBConstruct 1–381; UniProt 1–381

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 9qwu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9qwu
Deposition date deposition_date2025-04-15
Structure title titleCryo-EM structure of the human UBR4/KCMF1/CALM1 complex (CALM1 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_guinier49.83
Radius of gyration Rg (electron density) rg_electron49.35
Forward intensity I(0) i0837906000.00
Molecular weight molecular_weight242570.0 kDa
Excluded volume excluded_volume304780 ų
Envelope volume envelope_volume449360 ų
Hydration-shell volume shell_volume75959 ų
Envelope diameter envelope_diameter154.0
Shell Rg shell_rg52.51
Envelope Rg envelope_rg49.18
Shape Rg shape_rg49.42
Total Rg total_rg49.24
Total atoms total_atoms17031
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 dmax145.9
Rg (real space) rg_real49.62
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real8.3790e+08
I(0) uncertainty (real space) i0_real_error1.6020e+07
Rg (reciprocal space) rg_reciprocal49.83
I(0) (reciprocal space) i0_reciprocal838100000.0000
Solution quality estimate total_estimate0.8503
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.3
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.756
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha67280000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.996; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.061

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)