3dwh

Structural and Functional Analysis of SRA domain

Method: X-RAY DIFFRACTION Dmax: 62.2 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 414–617 Fragment:SRA domain, YDG Domain, residues 414-617 SO4 SULFATE ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;100mM Tris-Hcl 1.2M ammonium Sulfate 0.2M NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.95 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.

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 5–208; UniProt 414–617

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 3dwh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3dwh
Deposition date deposition_date2008-07-22
Structure title titleStructural and Functional Analysis of SRA domain
Keywords keywords;Beta Barrel, Cell cycle, DNA damage, DNA repair, DNA-binding, Ligase, Metal-binding, Nucleus, Phosphoprotein, Transcription, Transcription regulation, Ubl conjugation pathway, Zinc-finger ;; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.71
Radius of gyration Rg (electron density) rg_electron16.66
Forward intensity I(0) i09384920.00
Molecular weight molecular_weight21494.0 kDa
Excluded volume excluded_volume26434 ų
Envelope volume envelope_volume30923 ų
Hydration-shell volume shell_volume15713 ų
Envelope diameter envelope_diameter63.5
Shell Rg shell_rg22.68
Envelope Rg envelope_rg17.18
Shape Rg shape_rg16.63
Total Rg total_rg17.73
Total atoms total_atoms1516
Residues n_residues193
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 dmax62.2
Rg (real space) rg_real17.65
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real9.3850e+06
I(0) uncertainty (real space) i0_real_error1.1290e+05
Rg (reciprocal space) rg_reciprocal17.66
I(0) (reciprocal space) i0_reciprocal9385000.0000
Solution quality estimate total_estimate0.6074
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.2
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.143
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2688000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.684; Stabil: 0.999; Sysdev: 0.291; Positv: 1.000; Valcen: 0.971; 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_idd3dwha2
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_idd3dwha3
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_id3dwhA01
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)