5cvl

WDR48 (UAF-1), residues 2-580

Method: X-RAY DIFFRACTION Dmax: 89.2 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–580 Fragment:UNP residues 2-580 PO4 PHOSPHATE ION × 2 AU GOLD ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;292 K;0.72 M sodium phosphate, 0.72 M potassium phosphate, 90 mM HEPES pH 7.5 Resolution 3.00 Å R-free 0.233

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 25 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 17–595; UniProt 2–580

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 5cvl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5cvl
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5cvl
Deposition date deposition_date2015-07-27
Structure title titleWDR48 (UAF-1), residues 2-580
Keywords keywordsWDR48, UAF1, WD-repeat, USP, deubiquitinase, DUB, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.30
Radius of gyration Rg (electron density) rg_electron25.55
Forward intensity I(0) i065922200.00
Molecular weight molecular_weight60449.0 kDa
Excluded volume excluded_volume74020 ų
Envelope volume envelope_volume89733 ų
Hydration-shell volume shell_volume29316 ų
Envelope diameter envelope_diameter93.2
Shell Rg shell_rg32.74
Envelope Rg envelope_rg25.91
Shape Rg shape_rg25.54
Total Rg total_rg26.30
Total atoms total_atoms4155
Residues n_residues526
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 dmax89.2
Rg (real space) rg_real26.32
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real6.5920e+07
I(0) uncertainty (real space) i0_real_error1.0270e+06
Rg (reciprocal space) rg_reciprocal26.31
I(0) (reciprocal space) i0_reciprocal65920000.0000
Solution quality estimate total_estimate0.8767
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.406
Kurtosis Kurtosis kurtosis-0.234
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha9788000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)