6vfo

Solution structure of the PHD of mouse UHRF1 (NP95)

Method: SOLUTION NMR Dmax: 59.1 Å Quality: REASONABLE

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

E3 ubiquitin-protein ligase UHRF1

Mus musculus

UniProt Q8VDF2

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 303–380 Not recorded ZN ZINC ION × 3 SOLUTION NMR NMR measurement conditions:pH 7.5;290 K;Ionic strength (raw mmCIF value) 150;Pressure 1 NMR sample composition:200 uM [U-99% 13C; U-99% 15N] PHD, 5 mM DTT, 2 mM beta-mercaptoethanol, 5 mM TCEP, 150 mM sodium chloride, 50 mM sodium phosphate, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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.

18 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UHRF1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–78; UniProt 303–380

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 6vfo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6vfo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6vfo
Deposition date deposition_date2020-01-06
Structure title titleSolution structure of the PHD of mouse UHRF1 (NP95)
Keywords keywordsHistone, Plant Homeodomain, NP95, H3K9me3, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.01
Radius of gyration Rg (electron density) rg_electron14.12
Forward intensity I(0) i0558565000.00
Molecular weight molecular_weight176840.0 kDa
Excluded volume excluded_volume211310 ų
Envelope volume envelope_volume36819 ų
Hydration-shell volume shell_volume16974 ų
Envelope diameter envelope_diameter66.2
Shell Rg shell_rg24.67
Envelope Rg envelope_rg19.50
Shape Rg shape_rg14.22
Total Rg total_rg14.09
Total atoms total_atoms23000
Residues n_residues1560
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 dmax59.1
Rg (real space) rg_real14.09
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real5.5860e+08
I(0) uncertainty (real space) i0_real_error7.3820e+06
Rg (reciprocal space) rg_reciprocal14.08
I(0) (reciprocal space) i0_reciprocal558600000.0000
Solution quality estimate total_estimate0.7285
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.7
Skewness Skewness skewness0.490
Kurtosis Kurtosis kurtosis0.063
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha139500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.374; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.344; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6vfoa_
Class classg — Small proteins
Fold Fold foldg.50 — FYVE/PHD zinc finger
Superfamily Superfamily superfamilyg.50.1 — FYVE/PHD zinc finger
Family Family familyg.50.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id6vfoA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily1150

8. Citations (1)

9. Files and Curves (10)