8qjr

BRG1 bromodomain in complex with VBC via compound 17

Method: X-RAY DIFFRACTION Dmax: 137.8 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–104 Not recorded Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) Transcription activator BRG1 × 1 (P51532) PO4 PHOSPHATE ION × 5 GOL GLYCEROL × 1 VLH (2S,4R)-1-[(2R)-2-[3-[2-[4-[3-[4-[(1R,5S)-3-[3-azanyl-6-(2-hydroxyphenyl)pyridazin-4-yl]-3,8-diazabicyclo[3.2.1]octan-8-yl]pyridin-2-yl]oxycyclobutyl]oxypiperidin-1-yl]ethoxy]-1,2-oxazol-5-yl]-3-methyl-butanoyl]-N-[(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;27 mM HEPES pH 6.8, 73 mM HEPES pH 8.6, 1.0 M NaI Resolution 3.17 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–104 Not recorded Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) Transcription activator BRG1 × 1 (P51532) PO4 PHOSPHATE ION × 2 VLH (2S,4R)-1-[(2R)-2-[3-[2-[4-[3-[4-[(1R,5S)-3-[3-azanyl-6-(2-hydroxyphenyl)pyridazin-4-yl]-3,8-diazabicyclo[3.2.1]octan-8-yl]pyridin-2-yl]oxycyclobutyl]oxypiperidin-1-yl]ethoxy]-1,2-oxazol-5-yl]-3-methyl-butanoyl]-N-[(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;27 mM HEPES pH 6.8, 73 mM HEPES pH 8.6, 1.0 M NaI Resolution 3.17 Å R-free 0.278

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 477 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

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 17–112 Not recorded Elongin-B × 1 (Q15370) von Hippel-Lindau disease tumor suppressor × 1 (P40337) Transcription activator BRG1 × 1 (P51532) PO4 PHOSPHATE ION × 5 GOL GLYCEROL × 1 VLH (2S,4R)-1-[(2R)-2-[3-[2-[4-[3-[4-[(1R,5S)-3-[3-azanyl-6-(2-hydroxyphenyl)pyridazin-4-yl]-3,8-diazabicyclo[3.2.1]octan-8-yl]pyridin-2-yl]oxycyclobutyl]oxypiperidin-1-yl]ethoxy]-1,2-oxazol-5-yl]-3-methyl-butanoyl]-N-[(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;27 mM HEPES pH 6.8, 73 mM HEPES pH 8.6, 1.0 M NaI Resolution 3.17 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 17–112 Not recorded Elongin-B × 1 (Q15370) von Hippel-Lindau disease tumor suppressor × 1 (P40337) Transcription activator BRG1 × 1 (P51532) PO4 PHOSPHATE ION × 2 VLH (2S,4R)-1-[(2R)-2-[3-[2-[4-[3-[4-[(1R,5S)-3-[3-azanyl-6-(2-hydroxyphenyl)pyridazin-4-yl]-3,8-diazabicyclo[3.2.1]octan-8-yl]pyridin-2-yl]oxycyclobutyl]oxypiperidin-1-yl]ethoxy]-1,2-oxazol-5-yl]-3-methyl-butanoyl]-N-[(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;27 mM HEPES pH 6.8, 73 mM HEPES pH 8.6, 1.0 M NaI Resolution 3.17 Å R-free 0.278

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 466 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

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 54–213 Not recorded Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Transcription activator BRG1 × 1 (P51532) PO4 PHOSPHATE ION × 5 GOL GLYCEROL × 1 VLH (2S,4R)-1-[(2R)-2-[3-[2-[4-[3-[4-[(1R,5S)-3-[3-azanyl-6-(2-hydroxyphenyl)pyridazin-4-yl]-3,8-diazabicyclo[3.2.1]octan-8-yl]pyridin-2-yl]oxycyclobutyl]oxypiperidin-1-yl]ethoxy]-1,2-oxazol-5-yl]-3-methyl-butanoyl]-N-[(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;27 mM HEPES pH 6.8, 73 mM HEPES pH 8.6, 1.0 M NaI Resolution 3.17 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 54–213 Not recorded Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) Transcription activator BRG1 × 1 (P51532) PO4 PHOSPHATE ION × 2 VLH (2S,4R)-1-[(2R)-2-[3-[2-[4-[3-[4-[(1R,5S)-3-[3-azanyl-6-(2-hydroxyphenyl)pyridazin-4-yl]-3,8-diazabicyclo[3.2.1]octan-8-yl]pyridin-2-yl]oxycyclobutyl]oxypiperidin-1-yl]ethoxy]-1,2-oxazol-5-yl]-3-methyl-butanoyl]-N-[(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;27 mM HEPES pH 6.8, 73 mM HEPES pH 8.6, 1.0 M NaI Resolution 3.17 Å R-free 0.278

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 362 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

Transcription activator BRG1

Homo sapiens

UniProt P51532

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 1418–1536 Fragment:UNP residues 1418-1536 Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) PO4 PHOSPHATE ION × 5 GOL GLYCEROL × 1 VLH (2S,4R)-1-[(2R)-2-[3-[2-[4-[3-[4-[(1R,5S)-3-[3-azanyl-6-(2-hydroxyphenyl)pyridazin-4-yl]-3,8-diazabicyclo[3.2.1]octan-8-yl]pyridin-2-yl]oxycyclobutyl]oxypiperidin-1-yl]ethoxy]-1,2-oxazol-5-yl]-3-methyl-butanoyl]-N-[(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;27 mM HEPES pH 6.8, 73 mM HEPES pH 8.6, 1.0 M NaI Resolution 3.17 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 1418–1536 Fragment:UNP residues 1418-1536 Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) PO4 PHOSPHATE ION × 2 VLH (2S,4R)-1-[(2R)-2-[3-[2-[4-[3-[4-[(1R,5S)-3-[3-azanyl-6-(2-hydroxyphenyl)pyridazin-4-yl]-3,8-diazabicyclo[3.2.1]octan-8-yl]pyridin-2-yl]oxycyclobutyl]oxypiperidin-1-yl]ethoxy]-1,2-oxazol-5-yl]-3-methyl-butanoyl]-N-[(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;27 mM HEPES pH 6.8, 73 mM HEPES pH 8.6, 1.0 M NaI Resolution 3.17 Å R-free 0.278

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.

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

View Construct and Data Evidence
UniProt name SMCA4_HUMAN
Isoform P51532-2
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 3–121; UniProt 1418–1536 Author chain H; PDBConstruct 3–121; UniProt 1418–1536

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 8qjr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8qjr
Deposition date deposition_date2023-09-13
Structure title titleBRG1 bromodomain in complex with VBC via compound 17
Keywords keywordsBRG1, BROMODOMAIN, VHL, ELONGIN, VBC, E3 LIGASE, VON HIPPEL-LINDAU, UBIQUITINASE, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.99
Radius of gyration Rg (electron density) rg_electron39.91
Forward intensity I(0) i0171203000.00
Molecular weight molecular_weight106560.0 kDa
Excluded volume excluded_volume133830 ų
Envelope volume envelope_volume193110 ų
Hydration-shell volume shell_volume42768 ų
Envelope diameter envelope_diameter135.5
Shell Rg shell_rg42.34
Envelope Rg envelope_rg39.77
Shape Rg shape_rg39.88
Total Rg total_rg40.17
Total atoms total_atoms7486
Residues n_residues898
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 dmax137.8
Rg (real space) rg_real40.02
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real1.7120e+08
I(0) uncertainty (real space) i0_real_error2.7720e+06
Rg (reciprocal space) rg_reciprocal40.01
I(0) (reciprocal space) i0_reciprocal171200000.0000
Solution quality estimate total_estimate0.8822
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.7
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.472
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11280000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.869; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.938; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)