9yh8

M17T Human DJ-1

Method: X-RAY DIFFRACTION Dmax: 50.1 Å Quality: GOOD

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

Parkinson disease protein 7

Homo sapiens

UniProt Q99497

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–189 Mutation:M17T EDO 1,2-ETHANEDIOL × 10 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;19-22% PEG 4000, 200 mM MgCl2, and 100 mM Tris HCl, pH=8.5 Resolution 1.00 Å R-free 0.130

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.

87 other PDB entries and 97 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PARK7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–192; UniProt 1–189

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 9yh8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yh8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yh8
Deposition date deposition_date2025-09-30
Structure title titleM17T Human DJ-1
Keywords keywordsPARK7, glyoxalase, cyclic phosphoglycerate anhydride hydrolase, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.57
Radius of gyration Rg (electron density) rg_electron15.19
Forward intensity I(0) i07299400.00
Molecular weight molecular_weight19881.0 kDa
Excluded volume excluded_volume25065 ų
Envelope volume envelope_volume27851 ų
Hydration-shell volume shell_volume15137 ų
Envelope diameter envelope_diameter49.9
Shell Rg shell_rg21.48
Envelope Rg envelope_rg15.56
Shape Rg shape_rg15.18
Total Rg total_rg16.36
Total atoms total_atoms2844
Residues n_residues187
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 dmax50.1
Rg (real space) rg_real16.41
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real7.2990e+06
I(0) uncertainty (real space) i0_real_error7.7590e+04
Rg (reciprocal space) rg_reciprocal16.43
I(0) (reciprocal space) i0_reciprocal7299000.0000
Solution quality estimate total_estimate0.7755
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.1
Skewness Skewness skewness0.035
Kurtosis Kurtosis kurtosis-0.473
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1649000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 0.471; Positv: 1.000; Valcen: 0.977; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (2)

9. Files and Curves (10)