8hck

NMR fragment-based screening against the two PDZ do-mains of MDA-9

Method: X-RAY DIFFRACTION Dmax: 43.5 Å Quality: GOOD

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

Syntenin-1

Homo sapiens

UniProt O00560

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 113–191 Not recorded P1Z 4-BUTYL-1,2-DIPHENYL-PYRAZOLIDINE-3,5-DIONE × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;e.g.Cobalt chlonde hexahydrate, MES monohydrate, Ammouium sulfate. Resolution 2.00 Å R-free 0.264

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 186 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SDCB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–81; UniProt 113–191

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 8hck

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8hck
Deposition date deposition_date2022-11-01
Structure title titleNMR fragment-based screening against the two PDZ do-mains of MDA-9
Keywords keywordse.g.MDA-9, PDZdomain, inhibitor, therapeutic target, CELL INVASION; CELL INVASION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.40
Radius of gyration Rg (electron density) rg_electron11.83
Forward intensity I(0) i02022840.00
Molecular weight molecular_weight9462.0 kDa
Excluded volume excluded_volume11776 ų
Envelope volume envelope_volume13229 ų
Hydration-shell volume shell_volume9615 ų
Envelope diameter envelope_diameter41.8
Shell Rg shell_rg17.42
Envelope Rg envelope_rg12.20
Shape Rg shape_rg11.80
Total Rg total_rg13.26
Total atoms total_atoms660
Residues n_residues80
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 dmax43.5
Rg (real space) rg_real13.31
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real2.0230e+06
I(0) uncertainty (real space) i0_real_error2.3890e+04
Rg (reciprocal space) rg_reciprocal13.31
I(0) (reciprocal space) i0_reciprocal2023000.0000
Solution quality estimate total_estimate0.8724
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.6
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.267
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha545000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)