5l8e

Structure of UAF1

Method: X-RAY DIFFRACTION Dmax: 98.6 Å Quality: GOOD

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

WD repeat-containing protein 48

Homo sapiens

UniProt Q8TAF3

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 9–580 Not recorded Unknown × 1 GOL GLYCEROL × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;20% PEG3350, 200mM Tri-Sodium Citrate, Bis-Tris Propane Cryo -30% Glycerol Resolution 2.30 Å R-free 0.224
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 9–580 Not recorded GOL GLYCEROL × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;20% PEG3350, 200mM Tri-Sodium Citrate, Bis-Tris Propane Cryo -30% Glycerol Resolution 2.30 Å R-free 0.224

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR48_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–580; UniProt 9–580 Author chain B; PDBConstruct 9–580; UniProt 9–580

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 5l8e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5l8e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5l8e
Deposition date deposition_date2016-06-07
Structure title titleStructure of UAF1
Keywords keywordsWDR48 Activates USP1/12/46 B propellar, structural protein; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.30
Radius of gyration Rg (electron density) rg_electron31.28
Forward intensity I(0) i0218817000.00
Molecular weight molecular_weight117540.0 kDa
Excluded volume excluded_volume146970 ų
Envelope volume envelope_volume183940 ų
Hydration-shell volume shell_volume47429 ų
Envelope diameter envelope_diameter99.5
Shell Rg shell_rg39.80
Envelope Rg envelope_rg31.33
Shape Rg shape_rg31.24
Total Rg total_rg32.08
Total atoms total_atoms8253
Residues n_residues1039
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 dmax98.6
Rg (real space) rg_real32.12
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real2.1880e+08
I(0) uncertainty (real space) i0_real_error3.2230e+06
Rg (reciprocal space) rg_reciprocal32.20
I(0) (reciprocal space) i0_reciprocal218800000.0000
Solution quality estimate total_estimate0.8337
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.2
Skewness Skewness skewness0.146
Kurtosis Kurtosis kurtosis-0.601
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha85550000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)