8wms

Crystal structure of human DPPA3 in complex with human UHRF1 PHD domain

Method: X-RAY DIFFRACTION Dmax: 56.8 Å Quality: GOOD

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

E3 ubiquitin-protein ligase UHRF1

Homo sapiens

UniProt Q96T88

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 299–366 Not recorded Developmental pluripotency-associated protein 3 × 1 (Q6W0C5) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;100 mM Tris-HCl (pH 7.0), 200 mM tri-potassium phosphate and 20% (w/v) PEG3,350 Resolution 2.40 Å R-free 0.266

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.

44 other PDB entries and 76 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UHRF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–68; UniProt 299–366

Developmental pluripotency-associated protein 3

Homo sapiens

UniProt Q6W0C5

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 81–118 Not recorded E3 ubiquitin-protein ligase UHRF1 × 1 (Q96T88) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;100 mM Tris-HCl (pH 7.0), 200 mM tri-potassium phosphate and 20% (w/v) PEG3,350 Resolution 2.40 Å R-free 0.266

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.

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

View Construct and Data Evidence
UniProt name DPPA3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–38; UniProt 81–118

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 8wms

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wms
Deposition date deposition_date2023-10-04
Structure title titleCrystal structure of human DPPA3 in complex with human UHRF1 PHD domain
Keywords keywordsDNA methylation, 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_guinier14.70
Radius of gyration Rg (electron density) rg_electron14.12
Forward intensity I(0) i02814930.00
Molecular weight molecular_weight10525.0 kDa
Excluded volume excluded_volume12614 ų
Envelope volume envelope_volume15274 ų
Hydration-shell volume shell_volume9802 ų
Envelope diameter envelope_diameter52.5
Shell Rg shell_rg18.95
Envelope Rg envelope_rg14.70
Shape Rg shape_rg14.16
Total Rg total_rg15.00
Total atoms total_atoms707
Residues n_residues89
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 dmax56.8
Rg (real space) rg_real14.71
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real2.8150e+06
I(0) uncertainty (real space) i0_real_error3.4220e+04
Rg (reciprocal space) rg_reciprocal14.71
I(0) (reciprocal space) i0_reciprocal2815000.0000
Solution quality estimate total_estimate0.7987
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.3
Skewness Skewness skewness0.375
Kurtosis Kurtosis kurtosis-0.132
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha241600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.538; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.766; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)