9uth

DPF3b in complex with H3K14cr peptide

Method: X-RAY DIFFRACTION Dmax: 100.9 Å Quality: GOOD

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

Zinc finger protein DPF3

Homo sapiens

UniProt Q92784

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 255–368 Chain C; UniProt 255–368 Not recorded Histone H3.3 × 2 (P84243) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277.15 K;4 M Sodium Formate, pH 7.0 Resolution 2.69 Å R-free 0.230
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 255–368 Chain G; UniProt 255–368 Not recorded Histone H3.3 × 2 (P84243) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277.15 K;4 M Sodium Formate, pH 7.0 Resolution 2.69 Å R-free 0.230

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.

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPF3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–114; UniProt 255–368 Author chain C; PDBConstruct 1–114; UniProt 255–368 Author chain E; PDBConstruct 1–114; UniProt 255–368 Author chain G; PDBConstruct 1–114; UniProt 255–368

Histone H3.3

Homo sapiens

UniProt P84243

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 2–27 Chain D; UniProt 2–27 Non-standard monomer:Yes (specific site not provided by mmCIF) Zinc finger protein DPF3 × 2 (Q92784) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277.15 K;4 M Sodium Formate, pH 7.0 Resolution 2.69 Å R-free 0.230
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 2–27 Chain H; UniProt 2–27 Non-standard monomer:Yes (specific site not provided by mmCIF) Zinc finger protein DPF3 × 2 (Q92784) ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277.15 K;4 M Sodium Formate, pH 7.0 Resolution 2.69 Å R-free 0.230

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.

94 other PDB entries and 122 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H33_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–26; UniProt 2–27 Author chain D; PDBConstruct 1–26; UniProt 2–27 Author chain F; PDBConstruct 1–26; UniProt 2–27 Author chain H; PDBConstruct 1–26; UniProt 2–27

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 9uth

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9uth
Deposition date deposition_date2025-05-03
最后修订 last_revision2026-05-06
Structure title titleDPF3b in complex with H3K14cr peptide
Keywords keywordsDPF3b, H3K14 crotonylation, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.27
Radius of gyration Rg (electron density) rg_electron31.09
Forward intensity I(0) i074663800.00
Molecular weight molecular_weight62638.0 kDa
Excluded volume excluded_volume75795 ų
Envelope volume envelope_volume103510 ų
Hydration-shell volume shell_volume28798 ų
Envelope diameter envelope_diameter106.9
Shell Rg shell_rg36.95
Envelope Rg envelope_rg30.36
Shape Rg shape_rg31.08
Total Rg total_rg31.62
Total atoms total_atoms4286
Residues n_residues553
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 dmax100.9
Rg (real space) rg_real31.44
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real7.4660e+07
I(0) uncertainty (real space) i0_real_error1.0910e+06
Rg (reciprocal space) rg_reciprocal31.38
I(0) (reciprocal space) i0_reciprocal74660000.0000
Solution quality estimate total_estimate0.8727
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.7
Skewness Skewness skewness0.357
Kurtosis Kurtosis kurtosis-0.711
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7001000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.778; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)