10ap

Crystal Structure of Human WRN helicase with compound 26

Method: X-RAY DIFFRACTION Dmax: 85.1 Å Quality: GOOD

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

;Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN ;

Homo sapiens

UniProt Q14191

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 500–946 Not recorded A1C4O (2R)-N-[(3R)-1,1-dioxo-1lambda~6~-thiolan-3-yl]-N-{[2-(2-hydroxypropan-2-yl)pyridin-4-yl]methyl}-2-methoxy-2-[(1M)-3,3',4'-trifluoro[1,1'-biphenyl]-4-yl]acetamide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;277 K;co-crystallization additive 46 [Proplex-E2-B4+29% glycerol] Resolution 2.58 Å R-free 0.286

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.

49 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WRN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–447; UniProt 500–946

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 10ap

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10ap
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10ap
Deposition date deposition_date2026-01-08
Structure title titleCrystal Structure of Human WRN helicase with compound 26
Keywords keywordsDNA helicase RecQ family allosteric inhibitor, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.70
Radius of gyration Rg (electron density) rg_electron24.07
Forward intensity I(0) i079099500.00
Molecular weight molecular_weight45849.0 kDa
Excluded volume excluded_volume43888 ų
Envelope volume envelope_volume75656 ų
Hydration-shell volume shell_volume26439 ų
Envelope diameter envelope_diameter88.6
Shell Rg shell_rg31.00
Envelope Rg envelope_rg24.17
Shape Rg shape_rg24.07
Total Rg total_rg24.64
Total atoms total_atoms3444
Residues n_residues421
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 dmax85.1
Rg (real space) rg_real24.70
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real7.9100e+07
I(0) uncertainty (real space) i0_real_error1.1620e+06
Rg (reciprocal space) rg_reciprocal24.70
I(0) (reciprocal space) i0_reciprocal79100000.0000
Solution quality estimate total_estimate0.7897
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.371
Kurtosis Kurtosis kurtosis-0.310
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11120000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.781; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.936; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)