9hyo

CRYSTAL STRUCTURE OF THE SMARCA2-VCB-COMPLEX WITH PROTAC P4

Method: X-RAY DIFFRACTION Dmax: 99.3 Å Quality: GOOD

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

Probable global transcription activator SNF2L2

Homo sapiens

UniProt P51531

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 1373–1493 Not recorded Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1IYN (2~{S},4~{R})-~{N}-[[2-[2-[2-[2-[4-[7-(5-bromanyl-4-oxidanylidene-2,3-dihydro-1,3-benzoxazin-2-yl)-4-[cyclopropyl(methyl)amino]-5,6,8,9-tetrahydropyrimido[4,5-d]azepin-2-yl]piperazin-1-yl]ethoxy]ethoxy]ethoxy]-4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-1-[(2~{S})-2-[(1-fluoranylcyclopropyl)carbonylamino]-3,3-dimethyl-butanoyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES pH 7.0 8% ethylene glycol 14% PEG 8K Resolution 3.74 Å R-free 0.348

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 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMCA2_HUMAN
Isoform P51531-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–123; UniProt 1373–1493

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 B; UniProt 1–104 Not recorded Probable global transcription activator SNF2L2 × 1 (P51531) Elongin-C × 1 (Q15369) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1IYN (2~{S},4~{R})-~{N}-[[2-[2-[2-[2-[4-[7-(5-bromanyl-4-oxidanylidene-2,3-dihydro-1,3-benzoxazin-2-yl)-4-[cyclopropyl(methyl)amino]-5,6,8,9-tetrahydropyrimido[4,5-d]azepin-2-yl]piperazin-1-yl]ethoxy]ethoxy]ethoxy]-4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-1-[(2~{S})-2-[(1-fluoranylcyclopropyl)carbonylamino]-3,3-dimethyl-butanoyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES pH 7.0 8% ethylene glycol 14% PEG 8K Resolution 3.74 Å R-free 0.348

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 2
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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 17–112 Not recorded Probable global transcription activator SNF2L2 × 1 (P51531) Elongin-B × 1 (Q15370) von Hippel-Lindau disease tumor suppressor × 1 (P40337) A1IYN (2~{S},4~{R})-~{N}-[[2-[2-[2-[2-[4-[7-(5-bromanyl-4-oxidanylidene-2,3-dihydro-1,3-benzoxazin-2-yl)-4-[cyclopropyl(methyl)amino]-5,6,8,9-tetrahydropyrimido[4,5-d]azepin-2-yl]piperazin-1-yl]ethoxy]ethoxy]ethoxy]-4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-1-[(2~{S})-2-[(1-fluoranylcyclopropyl)carbonylamino]-3,3-dimethyl-butanoyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES pH 7.0 8% ethylene glycol 14% PEG 8K Resolution 3.74 Å R-free 0.348

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 C; 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 D; UniProt 54–213 Not recorded Probable global transcription activator SNF2L2 × 1 (P51531) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) A1IYN (2~{S},4~{R})-~{N}-[[2-[2-[2-[2-[4-[7-(5-bromanyl-4-oxidanylidene-2,3-dihydro-1,3-benzoxazin-2-yl)-4-[cyclopropyl(methyl)amino]-5,6,8,9-tetrahydropyrimido[4,5-d]azepin-2-yl]piperazin-1-yl]ethoxy]ethoxy]ethoxy]-4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-1-[(2~{S})-2-[(1-fluoranylcyclopropyl)carbonylamino]-3,3-dimethyl-butanoyl]-4-oxidanyl-pyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES pH 7.0 8% ethylene glycol 14% PEG 8K Resolution 3.74 Å R-free 0.348

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 D; 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 9hyo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9hyo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9hyo
Deposition date deposition_date2025-01-10
最后修订 last_revision2025-10-22
Structure title titleCRYSTAL STRUCTURE OF THE SMARCA2-VCB-COMPLEX WITH PROTAC P4
Keywords keywordsBromodomain, Complex, PROTAC, E3-Ligase, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.82
Radius of gyration Rg (electron density) rg_electron28.43
Forward intensity I(0) i085041100.00
Molecular weight molecular_weight48638.0 kDa
Excluded volume excluded_volume47077 ų
Envelope volume envelope_volume83917 ų
Hydration-shell volume shell_volume26289 ų
Envelope diameter envelope_diameter106.3
Shell Rg shell_rg33.44
Envelope Rg envelope_rg28.39
Shape Rg shape_rg28.43
Total Rg total_rg28.83
Total atoms total_atoms3685
Residues n_residues449
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 dmax99.3
Rg (real space) rg_real28.98
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real8.5040e+07
I(0) uncertainty (real space) i0_real_error1.4630e+06
Rg (reciprocal space) rg_reciprocal28.91
I(0) (reciprocal space) i0_reciprocal85040000.0000
Solution quality estimate total_estimate0.8543
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.488
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8105000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.814; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.751; Smooth: 0.910

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)