8zv8

Crystal structure of VHL-EloB-EloC in complex with a fragment compound 7HC_2 (D7)

Method: X-RAY DIFFRACTION Dmax: 127.3 Å Quality: GOOD

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–104 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–104 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–104 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 1–104 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287

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 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–104; UniProt 1–104 Author chain D; PDBConstruct 1–104; UniProt 1–104 Author chain G; PDBConstruct 1–104; UniProt 1–104 Author chain J; 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 17–112 Not recorded Elongin-B × 1 (Q15370) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 17–112 Not recorded Elongin-B × 1 (Q15370) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 17–112 Not recorded Elongin-B × 1 (Q15370) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain K; UniProt 17–112 Not recorded Elongin-B × 1 (Q15370) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287

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 464 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–97; UniProt 17–112 Author chain E; PDBConstruct 2–97; UniProt 17–112 Author chain H; PDBConstruct 2–97; UniProt 17–112 Author chain K; PDBConstruct 2–97; UniProt 17–112

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 54–213 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 54–213 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 54–213 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain L; UniProt 54–213 Non-standard monomer:Yes (specific site not provided by mmCIF) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) A1L2C 4-(hydroxymethyl)-7-oxidanyl-chromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;287 K;12% PEG 8K, 0.1 M Na cacodylate-HCl pH 6.0, 0.2 M Mg acetate, 5 mM DTT Resolution 2.46 Å R-free 0.287

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 360 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 C; PDBConstruct 3–162; UniProt 54–213 Author chain F; PDBConstruct 3–162; UniProt 54–213 Author chain I; PDBConstruct 3–162; UniProt 54–213 Author chain L; PDBConstruct 3–162; UniProt 54–213

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 8zv8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zv8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zv8
Deposition date deposition_date2024-06-11
Structure title titleCrystal structure of VHL-EloB-EloC in complex with a fragment compound 7HC_2 (D7)
Keywords keywordsE3 ligase, PROTAC, VHL, EloB, EloC, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.44
Radius of gyration Rg (electron density) rg_electron40.85
Forward intensity I(0) i0624395000.00
Molecular weight molecular_weight136040.0 kDa
Excluded volume excluded_volume131450 ų
Envelope volume envelope_volume273380 ų
Hydration-shell volume shell_volume55806 ų
Envelope diameter envelope_diameter133.9
Shell Rg shell_rg47.11
Envelope Rg envelope_rg39.01
Shape Rg shape_rg40.84
Total Rg total_rg41.14
Total atoms total_atoms10262
Residues n_residues1251
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 dmax127.3
Rg (real space) rg_real41.25
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real6.2440e+08
I(0) uncertainty (real space) i0_real_error1.0610e+07
Rg (reciprocal space) rg_reciprocal41.44
I(0) (reciprocal space) i0_reciprocal624500000.0000
Solution quality estimate total_estimate0.8830
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.0
Skewness Skewness skewness0.072
Kurtosis Kurtosis kurtosis-0.409
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14380000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.799

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)