9pku

Crystal Structure of YEATS domain of human YEATS2 in complex with LS-131 peptide

Method: X-RAY DIFFRACTION Dmax: 91.3 Å Quality: REASONABLE

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

YEATS domain-containing protein 2

Homo sapiens

UniProt Q9ULM3

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 201–332 Chain C; UniProt 201–332 Not recorded LS-131 peptide × 2 GOL GLYCEROL × 8 BZ2 1-benzofuran-2-carboxylic acid × 2 CL CHLORIDE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.8;291 K;2.0 M Sodium chloride, 0.1 M bis-tris propane pH 7.8 Resolution 2.88 Å R-free 0.251

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.

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YETS2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–135; UniProt 201–332 Author chain C; PDBConstruct 4–135; UniProt 201–332

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 9pku

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9pku
Deposition date deposition_date2025-07-14
最后修订 last_revision2026-01-07
Structure title titleCrystal Structure of YEATS domain of human YEATS2 in complex with LS-131 peptide
Keywords keywordsATAC complex, YEATS2, chemical probe, 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_guinier23.54
Radius of gyration Rg (electron density) rg_electron22.94
Forward intensity I(0) i036846900.00
Molecular weight molecular_weight31188.0 kDa
Excluded volume excluded_volume30058 ų
Envelope volume envelope_volume52732 ų
Hydration-shell volume shell_volume19953 ų
Envelope diameter envelope_diameter88.5
Shell Rg shell_rg28.70
Envelope Rg envelope_rg23.50
Shape Rg shape_rg22.93
Total Rg total_rg23.53
Total atoms total_atoms2370
Residues n_residues270
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 dmax91.3
Rg (real space) rg_real23.65
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real3.6850e+07
I(0) uncertainty (real space) i0_real_error5.8610e+05
Rg (reciprocal space) rg_reciprocal23.62
I(0) (reciprocal space) i0_reciprocal36850000.0000
Solution quality estimate total_estimate0.7147
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.460
Kurtosis Kurtosis kurtosis-0.161
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10770000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.578; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.552; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)