8wdk

The complex structure of Cul2-VCB-Protac-Wee1

Method: ELECTRON MICROSCOPY Dmax: 160.5 Å Quality: REASONABLE

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–745 Not recorded E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) von Hippel-Lindau disease tumor suppressor × 1 (P40337) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Wee1-like protein kinase × 1 (P30291) W6U (2S,4R)-1-[(2S)-3,3-dimethyl-2-[3-[4-[4-[4-[[3-oxidanylidene-1-[6-(2-oxidanylpropan-2-yl)pyridin-2-yl]-2-prop-2-enyl-pyrazolo[3,4-d]pyrimidin-6-yl]amino]phenyl]piperazin-1-yl]butoxy]propanoylamino]butanoyl]-N-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.64 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 1–745; UniProt 1–745

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain R; UniProt 21–102 Not recorded Cullin-2 × 1 (Q13617) von Hippel-Lindau disease tumor suppressor × 1 (P40337) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Wee1-like protein kinase × 1 (P30291) W6U (2S,4R)-1-[(2S)-3,3-dimethyl-2-[3-[4-[4-[4-[[3-oxidanylidene-1-[6-(2-oxidanylpropan-2-yl)pyridin-2-yl]-2-prop-2-enyl-pyrazolo[3,4-d]pyrimidin-6-yl]amino]phenyl]piperazin-1-yl]butoxy]propanoylamino]butanoyl]-N-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.64 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 2
Chains and sequence ranges Author chain R; PDBConstruct 1–82; UniProt 21–102

von Hippel-Lindau disease tumor suppressor

Homo sapiens

UniProt P40337

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 V; UniProt 59–213 Not recorded Cullin-2 × 1 (Q13617) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Wee1-like protein kinase × 1 (P30291) W6U (2S,4R)-1-[(2S)-3,3-dimethyl-2-[3-[4-[4-[4-[[3-oxidanylidene-1-[6-(2-oxidanylpropan-2-yl)pyridin-2-yl]-2-prop-2-enyl-pyrazolo[3,4-d]pyrimidin-6-yl]amino]phenyl]piperazin-1-yl]butoxy]propanoylamino]butanoyl]-N-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.64 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.

141 other PDB entries and 363 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VHL_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain V; PDBConstruct 1–155; UniProt 59–213

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–104 Not recorded Cullin-2 × 1 (Q13617) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) von Hippel-Lindau disease tumor suppressor × 1 (P40337) Elongin-C × 1 (Q15369) Wee1-like protein kinase × 1 (P30291) W6U (2S,4R)-1-[(2S)-3,3-dimethyl-2-[3-[4-[4-[4-[[3-oxidanylidene-1-[6-(2-oxidanylpropan-2-yl)pyridin-2-yl]-2-prop-2-enyl-pyrazolo[3,4-d]pyrimidin-6-yl]amino]phenyl]piperazin-1-yl]butoxy]propanoylamino]butanoyl]-N-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.64 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 B; PDBConstruct 1–104; UniProt 1–104

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–96 Not recorded Cullin-2 × 1 (Q13617) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) von Hippel-Lindau disease tumor suppressor × 1 (P40337) Elongin-B × 1 (Q15370) Wee1-like protein kinase × 1 (P30291) W6U (2S,4R)-1-[(2S)-3,3-dimethyl-2-[3-[4-[4-[4-[[3-oxidanylidene-1-[6-(2-oxidanylpropan-2-yl)pyridin-2-yl]-2-prop-2-enyl-pyrazolo[3,4-d]pyrimidin-6-yl]amino]phenyl]piperazin-1-yl]butoxy]propanoylamino]butanoyl]-N-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.64 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 Q15369-2
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 1–96; UniProt 1–96

Wee1-like protein kinase

Homo sapiens

UniProt P30291

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 W; UniProt 291–575 Not recorded Cullin-2 × 1 (Q13617) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 1 (P62877) von Hippel-Lindau disease tumor suppressor × 1 (P40337) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) W6U (2S,4R)-1-[(2S)-3,3-dimethyl-2-[3-[4-[4-[4-[[3-oxidanylidene-1-[6-(2-oxidanylpropan-2-yl)pyridin-2-yl]-2-prop-2-enyl-pyrazolo[3,4-d]pyrimidin-6-yl]amino]phenyl]piperazin-1-yl]butoxy]propanoylamino]butanoyl]-N-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.64 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.

28 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WEE1_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain W; PDBConstruct 2–286; UniProt 291–575

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 8wdk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wdk
Deposition date deposition_date2023-09-15
Structure title titleThe complex structure of Cul2-VCB-Protac-Wee1
Keywords keywordsE3 ligase complex, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.02
Radius of gyration Rg (electron density) rg_electron53.79
Forward intensity I(0) i0399717000.00
Molecular weight molecular_weight166750.0 kDa
Excluded volume excluded_volume208820 ų
Envelope volume envelope_volume361320 ų
Hydration-shell volume shell_volume56520 ų
Envelope diameter envelope_diameter169.0
Shell Rg shell_rg58.92
Envelope Rg envelope_rg50.25
Shape Rg shape_rg53.78
Total Rg total_rg54.01
Total atoms total_atoms11714
Residues n_residues1436
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 dmax160.5
Rg (real space) rg_real54.92
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real3.9570e+08
I(0) uncertainty (real space) i0_real_error5.7700e+06
Rg (reciprocal space) rg_reciprocal54.04
I(0) (reciprocal space) i0_reciprocal399800000.0000
Solution quality estimate total_estimate0.6613
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary83.0
Skewness Skewness skewness0.108
Kurtosis Kurtosis kurtosis-0.707
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha1.4680
Highest regularization parameter α highest_alpha16620000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.959; Stabil: 0.908; Sysdev: 0.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.033

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)