8xv8

Crystal structure of PHD domain of UHRF1 in complex with hStella peptide (residues 75-121)

Method: X-RAY DIFFRACTION Dmax: 121.2 Å Quality: REASONABLE

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 298–367 Fragment:PHD domain Developmental pluripotency-associated protein 3 × 1 (Q6W0C5) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M Ammonium acetate, 0.1 M HEPES pH 7.5, 25% PEG 3350 Resolution 2.05 Å R-free 0.207
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 298–367 Fragment:PHD domain Developmental pluripotency-associated protein 3 × 1 (Q6W0C5) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M Ammonium acetate, 0.1 M HEPES pH 7.5, 25% PEG 3350 Resolution 2.05 Å R-free 0.207
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 298–367 Fragment:PHD domain Developmental pluripotency-associated protein 3 × 1 (Q6W0C5) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M Ammonium acetate, 0.1 M HEPES pH 7.5, 25% PEG 3350 Resolution 2.05 Å R-free 0.207
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 298–367 Fragment:PHD domain Developmental pluripotency-associated protein 3 × 1 (Q6W0C5) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M Ammonium acetate, 0.1 M HEPES pH 7.5, 25% PEG 3350 Resolution 2.05 Å R-free 0.207

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 73 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 6–75; UniProt 298–367 Author chain C; PDBConstruct 6–75; UniProt 298–367 Author chain E; PDBConstruct 6–75; UniProt 298–367 Author chain G; PDBConstruct 6–75; UniProt 298–367

Developmental pluripotency-associated protein 3

OrganismNot specified

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 75–121 Not recorded E3 ubiquitin-protein ligase UHRF1 × 1 (Q96T88) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M Ammonium acetate, 0.1 M HEPES pH 7.5, 25% PEG 3350 Resolution 2.05 Å R-free 0.207
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 75–121 Not recorded E3 ubiquitin-protein ligase UHRF1 × 1 (Q96T88) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M Ammonium acetate, 0.1 M HEPES pH 7.5, 25% PEG 3350 Resolution 2.05 Å R-free 0.207
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 75–121 Not recorded E3 ubiquitin-protein ligase UHRF1 × 1 (Q96T88) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M Ammonium acetate, 0.1 M HEPES pH 7.5, 25% PEG 3350 Resolution 2.05 Å R-free 0.207
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 75–121 Not recorded E3 ubiquitin-protein ligase UHRF1 × 1 (Q96T88) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;0.2 M Ammonium acetate, 0.1 M HEPES pH 7.5, 25% PEG 3350 Resolution 2.05 Å R-free 0.207

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 5 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 1–47; UniProt 75–121 Author chain D; PDBConstruct 1–47; UniProt 75–121 Author chain F; PDBConstruct 1–47; UniProt 75–121 Author chain H; PDBConstruct 1–47; UniProt 75–121

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 8xv8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xv8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8xv8
Deposition date deposition_date2024-01-14
Structure title titleCrystal structure of PHD domain of UHRF1 in complex with hStella peptide (residues 75-121)
Keywords keywordsInhibitor, complex, 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_guinier30.18
Radius of gyration Rg (electron density) rg_electron30.57
Forward intensity I(0) i040181300.00
Molecular weight molecular_weight44314.0 kDa
Excluded volume excluded_volume53286 ų
Envelope volume envelope_volume79889 ų
Hydration-shell volume shell_volume23203 ų
Envelope diameter envelope_diameter124.6
Shell Rg shell_rg34.83
Envelope Rg envelope_rg31.58
Shape Rg shape_rg30.70
Total Rg total_rg30.60
Total atoms total_atoms3007
Residues n_residues379
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 dmax121.2
Rg (real space) rg_real30.49
Rg uncertainty (real space) rg_real_error1.63
I(0) (real space) i0_real4.0180e+07
I(0) uncertainty (real space) i0_real_error6.2540e+05
Rg (reciprocal space) rg_reciprocal30.36
I(0) (reciprocal space) i0_reciprocal40180000.0000
Solution quality estimate total_estimate0.7465
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.518
Kurtosis Kurtosis kurtosis-0.233
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3864000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.479; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.273; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)