1soa

Human DJ-1 with sulfinic acid

Method: X-RAY DIFFRACTION Dmax: 50.7 Å Quality: GOOD

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

RNA-binding protein regulatory subunit; oncogene DJ1

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 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;peg 400, sodium citrate, tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.20 Å R-free 0.141

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 1–189; 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 1soa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1soa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1soa
Deposition date deposition_date2004-03-13
Structure title titleHuman DJ-1 with sulfinic acid
Keywords keywords;Parkinson's disease, DJ-1/ThiJ/pfpI familiy, 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_guinier16.59
Radius of gyration Rg (electron density) rg_electron15.21
Forward intensity I(0) i07195610.00
Molecular weight molecular_weight19645.0 kDa
Excluded volume excluded_volume24768 ų
Envelope volume envelope_volume27652 ų
Hydration-shell volume shell_volume15044 ų
Envelope diameter envelope_diameter51.0
Shell Rg shell_rg21.43
Envelope Rg envelope_rg15.59
Shape Rg shape_rg15.20
Total Rg total_rg16.40
Total atoms total_atoms1376
Residues n_residues186
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 dmax50.7
Rg (real space) rg_real16.44
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real7.1960e+06
I(0) uncertainty (real space) i0_real_error8.1710e+04
Rg (reciprocal space) rg_reciprocal16.46
I(0) (reciprocal space) i0_reciprocal7196000.0000
Solution quality estimate total_estimate0.8954
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.041
Kurtosis Kurtosis kurtosis-0.465
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1654000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1soaa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.16 — Class I glutamine amidotransferase-like
Family Family familyc.23.16.2 — DJ-1/PfpI

CATH v4.4 (1 domains)

Domain ID domain_id1soaA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily880 — Class I glutamine amidotransferase (GATase) domain

8. Citations (2)

9. Files and Curves (10)