9uk3

Crystal structure of WDR5 in complex with peptide Ac-MRTEPRPPAP-NH2

Method: X-RAY DIFFRACTION Dmax: 52.9 Å Quality: GOOD

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

SCRIB overlapping open reading frame protein

OrganismNot specified

UniProt C0HLS1

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 B; UniProt 1–10 Non-standard monomer:Yes (specific site not provided by mmCIF) WD repeat-containing protein 5 × 1 (P61964) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291.15 K;0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350 Resolution 1.69 Å R-free 0.200

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OSCRI_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 2–11; UniProt 1–10

WD repeat-containing protein 5

Homo sapiens

UniProt P61964

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 22–334 Not recorded SCRIB overlapping open reading frame protein × 1 (C0HLS1) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291.15 K;0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350 Resolution 1.69 Å R-free 0.200

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.

198 other PDB entries and 294 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–313; UniProt 22–334

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 9uk3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9uk3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9uk3
Deposition date deposition_date2025-04-17
Structure title titleCrystal structure of WDR5 in complex with peptide Ac-MRTEPRPPAP-NH2
Keywords keywordsWD repeat, WIN site, MLL complex, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.56
Radius of gyration Rg (electron density) rg_electron17.60
Forward intensity I(0) i018952700.00
Molecular weight molecular_weight33844.0 kDa
Excluded volume excluded_volume42487 ų
Envelope volume envelope_volume44784 ų
Hydration-shell volume shell_volume20475 ų
Envelope diameter envelope_diameter54.2
Shell Rg shell_rg24.64
Envelope Rg envelope_rg17.74
Shape Rg shape_rg17.57
Total Rg total_rg18.58
Total atoms total_atoms2385
Residues n_residues311
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 dmax52.9
Rg (real space) rg_real18.40
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real1.8950e+07
I(0) uncertainty (real space) i0_real_error2.1190e+05
Rg (reciprocal space) rg_reciprocal18.42
I(0) (reciprocal space) i0_reciprocal18950000.0000
Solution quality estimate total_estimate0.8350
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.032
Kurtosis Kurtosis kurtosis-0.543
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6396000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)