2zo0

mouse NP95 SRA domain DNA specific complex 1

Method: X-RAY DIFFRACTION Dmax: 64.2 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 419–628 Fragment:SRA domain, residues 419-628 ;DNA (5'-D(*DTP*DCP*DCP*DAP*DTP*DGP*DCP*DGP*DCP*DTP*DGP*DAP*DC)-3') ; × 1 ;DNA (5'-D(*DGP*DTP*DCP*DAP*DGP*(5CM)P*DGP*DCP*DAP*DAP*DTP*DGP*DG)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;289 K;20% (v/v) polyethylene glycol 3350, 0.4M NaCl, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.19 Å R-free 0.253
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 419–628 Fragment:SRA domain, residues 419-628 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;289 K;20% (v/v) polyethylene glycol 3350, 0.4M NaCl, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.19 Å R-free 0.253

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 27 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 3–212; UniProt 419–628

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 2zo0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2zo0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2zo0
Deposition date deposition_date2008-05-05
Structure title titlemouse NP95 SRA domain DNA specific complex 1
Keywords keywords;base flipping, Cell cycle, Developmental protein, DNA damage, DNA repair, DNA-binding, Ligase, Metal-binding, Nucleus, Phosphoprotein, Transcription, Transcription regulation, Ubl conjugation, Ubl conjugation pathway, Zinc, 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_guinier19.43
Radius of gyration Rg (electron density) rg_electron18.48
Forward intensity I(0) i023952400.00
Molecular weight molecular_weight30894.0 kDa
Excluded volume excluded_volume35872 ų
Envelope volume envelope_volume44163 ų
Hydration-shell volume shell_volume19846 ų
Envelope diameter envelope_diameter66.6
Shell Rg shell_rg25.03
Envelope Rg envelope_rg18.84
Shape Rg shape_rg18.42
Total Rg total_rg19.39
Total atoms total_atoms2149
Residues n_residues234
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 dmax64.2
Rg (real space) rg_real19.32
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real2.3950e+07
I(0) uncertainty (real space) i0_real_error2.8090e+05
Rg (reciprocal space) rg_reciprocal19.34
I(0) (reciprocal space) i0_reciprocal23950000.0000
Solution quality estimate total_estimate0.8020
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.0
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.312
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4035000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.808; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2zo0b1
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
Domain ID domain_idd2zo0b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2zo0B01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology280 — PUA domain-like
Homologous superfamily homologous superfamily10 — SRA-YDG

8. Citations (1)

9. Files and Curves (10)