3f8j

Mouse UHRF1 SRA domain bound with hemi-methylated CpG, crystal structure in space group C222(1)

Method: X-RAY DIFFRACTION Dmax: 60.6 Å Quality: GOOD

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–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain B; UniProt 417–628 Fragment:YDG domain: UNP residues 417-628 5'-D(*DCP*DCP*DAP*DTP*DGP*(5CM)P*DGP*DCP*DTP*DGP*DAP*DC)-3' × 1 5'-D(*DGP*DTP*DCP*DAP*DGP*DCP*DGP*DCP*DAP*DTP*DGP*DG)-3' × 1 GOL GLYCEROL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;277 K;20% PEG 3350, 0.4 M NaCl, pH 7.0, VAPOR DIFFUSION, temperature 277K Resolution 1.99 Å R-free 0.232

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 B; PDBConstruct 1–212; UniProt 417–628

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 3f8j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3f8j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3f8j
Deposition date deposition_date2008-11-12
Structure title titleMouse UHRF1 SRA domain bound with hemi-methylated CpG, crystal structure in space group C222(1)
Keywords keywords;UHRF1, SRA, base flipping, 5-methylcytosine, CpG methylation, Cell cycle, Developmental protein, DNA damage, DNA repair, DNA-binding, Ligase, Metal-binding, Nucleus, Phosphoprotein, Transcription, Transcription regulation, Ubl conjugation pathway, Zinc-finger, LIGASE-DNA COMPLEX ;; LIGASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.26
Radius of gyration Rg (electron density) rg_electron18.20
Forward intensity I(0) i023470600.00
Molecular weight molecular_weight30917.0 kDa
Excluded volume excluded_volume36110 ų
Envelope volume envelope_volume43517 ų
Hydration-shell volume shell_volume19746 ų
Envelope diameter envelope_diameter62.1
Shell Rg shell_rg24.72
Envelope Rg envelope_rg18.52
Shape Rg shape_rg18.15
Total Rg total_rg19.13
Total atoms total_atoms2150
Residues n_residues229
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 dmax60.6
Rg (real space) rg_real19.14
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real2.3470e+07
I(0) uncertainty (real space) i0_real_error3.0090e+05
Rg (reciprocal space) rg_reciprocal19.16
I(0) (reciprocal space) i0_reciprocal23470000.0000
Solution quality estimate total_estimate0.8961
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.176
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3448000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3f8jb_
Class classb — All beta proteins
Fold Fold foldb.122 — PUA domain-like
Superfamily Superfamily superfamilyb.122.1 — PUA domain-like
Family Family familyb.122.1.12 — SRA domain-like

CATH v4.4 (1 domains)

Domain ID domain_id3f8jB01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology280 — PUA domain-like
Homologous superfamily homologous superfamily10 — SRA-YDG

8. Citations (2)

9. Files and Curves (10)