8ok1

WD repeat containing protein 5 (WDR5)- N225A mutant

Method: X-RAY DIFFRACTION Dmax: 56.2 Å Quality: EXCELLENT

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

Glutathione S-transferase class-mu 26 kDa isozyme,WD repeat-containing protein 5

Mus musculus

UniProt P08515

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–218 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M HEPES pH 7.5, 50 mM ammonium sulfate, 24% PEG3350 Resolution 1.38 Å R-free 0.218

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.

64 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GST26_SCHJA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–232; UniProt 1–218

Glutathione S-transferase class-mu 26 kDa isozyme,WD repeat-containing protein 5

Mus musculus

UniProt P61965

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 32–334 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M HEPES pH 7.5, 50 mM ammonium sulfate, 24% PEG3350 Resolution 1.38 Å R-free 0.218

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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR5_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 253–555; UniProt 32–334

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 8ok1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ok1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ok1
Deposition date deposition_date2023-03-26
最后修订 last_revision2024-04-03
Structure title titleWD repeat containing protein 5 (WDR5)- N225A mutant
Keywords keywordsScaffold protein, complex component, WD40 repeat, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.80
Radius of gyration Rg (electron density) rg_electron17.84
Forward intensity I(0) i017960700.00
Molecular weight molecular_weight33002.0 kDa
Excluded volume excluded_volume41565 ų
Envelope volume envelope_volume45317 ų
Hydration-shell volume shell_volume20489 ų
Envelope diameter envelope_diameter57.3
Shell Rg shell_rg24.80
Envelope Rg envelope_rg18.00
Shape Rg shape_rg17.80
Total Rg total_rg18.90
Total atoms total_atoms2327
Residues n_residues302
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 dmax56.2
Rg (real space) rg_real18.65
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real1.7960e+07
I(0) uncertainty (real space) i0_real_error2.0880e+05
Rg (reciprocal space) rg_reciprocal18.67
I(0) (reciprocal space) i0_reciprocal17960000.0000
Solution quality estimate total_estimate0.9027
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.046
Kurtosis Kurtosis kurtosis-0.526
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4872000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)