8wqe

Cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CUX1 (conformation 1)

Method: ELECTRON MICROSCOPY Dmax: 205.0 Å Quality: GOOD

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

Cullin-2

Homo sapiens

UniProt Q13617

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 2–745 Chain C; UniProt 2–745 Not recorded Protein fem-1 homolog B × 2 (Q9UK73) Elongin-C × 2 (Q15369) Elongin-B × 2 (Q15370) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein CASP × 2 (Q13948) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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.

41 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–750; UniProt 2–745 Author chain C; PDBConstruct 22–750; UniProt 2–745

Protein fem-1 homolog B

Homo sapiens

UniProt Q9UK73

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1–627 Chain D; UniProt 1–627 Not recorded Cullin-2 × 2 (Q13617) Elongin-C × 2 (Q15369) Elongin-B × 2 (Q15370) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein CASP × 2 (Q13948) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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.

30 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FEM1B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–627; UniProt 1–627 Author chain D; PDBConstruct 1–627; UniProt 1–627

Elongin-C

Homo sapiens

UniProt Q15369

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain E; UniProt 17–112 Chain G; UniProt 17–112 Not recorded Cullin-2 × 2 (Q13617) Protein fem-1 homolog B × 2 (Q9UK73) Elongin-B × 2 (Q15370) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein CASP × 2 (Q13948) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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.

220 other PDB entries and 467 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–96; UniProt 17–112 Author chain G; PDBConstruct 1–96; UniProt 17–112

Elongin-B

Homo sapiens

UniProt Q15370

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain F; UniProt 1–118 Chain H; UniProt 1–118 Not recorded Cullin-2 × 2 (Q13617) Protein fem-1 homolog B × 2 (Q9UK73) Elongin-C × 2 (Q15369) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein CASP × 2 (Q13948) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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.

228 other PDB entries and 478 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–118; UniProt 1–118 Author chain H; PDBConstruct 1–118; UniProt 1–118

E3 ubiquitin-protein ligase RBX1, N-terminally processed

Homo sapiens

UniProt P62877

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain I; UniProt 16–108 Chain J; UniProt 16–108 Not recorded Cullin-2 × 2 (Q13617) Protein fem-1 homolog B × 2 (Q9UK73) Elongin-C × 2 (Q15369) Elongin-B × 2 (Q15370) Protein CASP × 2 (Q13948) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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.

99 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 4–96; UniProt 16–108 Author chain J; PDBConstruct 4–96; UniProt 16–108

Protein CASP

Homo sapiens

UniProt Q13948

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain K; UniProt 656–678 Chain L; UniProt 656–678 Not recorded Cullin-2 × 2 (Q13617) Protein fem-1 homolog B × 2 (Q9UK73) Elongin-C × 2 (Q15369) Elongin-B × 2 (Q15370) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CASP_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain K; PDBConstruct 9–31; UniProt 656–678 Author chain L; PDBConstruct 9–31; UniProt 656–678

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 8wqe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wqe
Deposition date deposition_date2023-10-11
Structure title titleCryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CUX1 (conformation 1)
Keywords keywordsE3 ubiquitin ligase, Pro/C-degron, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.92
Radius of gyration Rg (electron density) rg_electron57.01
Forward intensity I(0) i02034570000.00
Molecular weight molecular_weight374950.0 kDa
Excluded volume excluded_volume468610 ų
Envelope volume envelope_volume700790 ų
Hydration-shell volume shell_volume106820 ų
Envelope diameter envelope_diameter216.7
Shell Rg shell_rg56.07
Envelope Rg envelope_rg55.92
Shape Rg shape_rg57.02
Total Rg total_rg56.97
Total atoms total_atoms26301
Residues n_residues3275
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 dmax205.0
Rg (real space) rg_real57.00
Rg uncertainty (real space) rg_real_error2.15
I(0) (real space) i0_real2.0350e+09
I(0) uncertainty (real space) i0_real_error4.0970e+07
Rg (reciprocal space) rg_reciprocal56.85
I(0) (reciprocal space) i0_reciprocal2034000000.0000
Solution quality estimate total_estimate0.8496
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.9
Skewness Skewness skewness0.458
Kurtosis Kurtosis kurtosis0.081
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha150100000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.692; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)