8g1q

Co-crystal structure of Compound 1 in complex with the bromodomain of human SMARCA4 and pVHL:ElonginC:ElonginB

Method: X-RAY DIFFRACTION Dmax: 101.1 Å Quality: GOOD

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

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 H; UniProt 1447–1569 Not recorded Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) NA SODIUM ION × 1 YHB N-(2-{4-[(6M)-3-amino-6-(2-hydroxyphenyl)pyridazin-4-yl]piperazin-1-yl}pyridine-4-carbonyl)-3-methyl-L-valyl-(4R)-4-hydroxy-N-{(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl}-L-prolinamide × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;PEG 300 0.1M Bis-Tris 6.5 Resolution 3.73 Å R-free 0.326

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMCA4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain H; PDBConstruct 2–124; UniProt 1447–1569

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 Transcription activator BRG1 × 1 (P51532) Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) NA SODIUM ION × 1 YHB N-(2-{4-[(6M)-3-amino-6-(2-hydroxyphenyl)pyridazin-4-yl]piperazin-1-yl}pyridine-4-carbonyl)-3-methyl-L-valyl-(4R)-4-hydroxy-N-{(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl}-L-prolinamide × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;PEG 300 0.1M Bis-Tris 6.5 Resolution 3.73 Å R-free 0.326

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 Q15370-2
PDB entities 2
Chains and sequence ranges Author chain A; 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 Transcription activator BRG1 × 1 (P51532) Elongin-B × 1 (Q15370) von Hippel-Lindau disease tumor suppressor × 1 (P40337) NA SODIUM ION × 1 YHB N-(2-{4-[(6M)-3-amino-6-(2-hydroxyphenyl)pyridazin-4-yl]piperazin-1-yl}pyridine-4-carbonyl)-3-methyl-L-valyl-(4R)-4-hydroxy-N-{(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl}-L-prolinamide × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;PEG 300 0.1M Bis-Tris 6.5 Resolution 3.73 Å R-free 0.326

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 B; PDBConstruct 1–96; 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 56–213 Not recorded Transcription activator BRG1 × 1 (P51532) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) NA SODIUM ION × 1 YHB N-(2-{4-[(6M)-3-amino-6-(2-hydroxyphenyl)pyridazin-4-yl]piperazin-1-yl}pyridine-4-carbonyl)-3-methyl-L-valyl-(4R)-4-hydroxy-N-{(1S)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]ethyl}-L-prolinamide × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;PEG 300 0.1M Bis-Tris 6.5 Resolution 3.73 Å R-free 0.326

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 4
Chains and sequence ranges Author chain C; PDBConstruct 5–162; UniProt 56–213

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 8g1q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8g1q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8g1q
Deposition date deposition_date2023-02-02
Structure title titleCo-crystal structure of Compound 1 in complex with the bromodomain of human SMARCA4 and pVHL:ElonginC:ElonginB
Keywords keywordsTernary Complex, PROTACs, TRANSCRIPTION, 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_guinier30.44
Radius of gyration Rg (electron density) rg_electron29.99
Forward intensity I(0) i038634300.00
Molecular weight molecular_weight49200.0 kDa
Excluded volume excluded_volume61924 ų
Envelope volume envelope_volume85020 ų
Hydration-shell volume shell_volume25331 ų
Envelope diameter envelope_diameter104.6
Shell Rg shell_rg34.76
Envelope Rg envelope_rg30.02
Shape Rg shape_rg29.98
Total Rg total_rg30.53
Total atoms total_atoms3466
Residues n_residues433
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 dmax101.1
Rg (real space) rg_real30.68
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real3.8630e+07
I(0) uncertainty (real space) i0_real_error5.8060e+05
Rg (reciprocal space) rg_reciprocal30.58
I(0) (reciprocal space) i0_reciprocal38630000.0000
Solution quality estimate total_estimate0.8532
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.451
Kurtosis Kurtosis kurtosis-0.535
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6794000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.730; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8g1qB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A
Domain ID domain_id8g1qC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily780 — von Hippel-Lindau disease tumour suppressor, beta domain
Domain ID domain_id8g1qC02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology750 — Elongin C; Chain C, domain 1
Homologous superfamily homologous superfamily10 — von Hippel-Lindau disease tumour suppressor, alpha domain

8. Citations (1)

9. Files and Curves (10)