7v63

Structure of dimeric uPAR at low pH

Method: X-RAY DIFFRACTION Dmax: 90.7 Å Quality: GOOD

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

Urokinase plasminogen activator surface receptor

Homo sapiens

UniProt Q03405

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 23–299 Chain B; UniProt 23–299 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;295 K;1.8-2.2 M ammonium sulphate in 50 mM sodium acetate at pH 4.5-5.2 Resolution 2.91 Å R-free 0.273

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.

11 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UPAR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–279; UniProt 23–299 Author chain B; PDBConstruct 3–279; UniProt 23–299

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 7v63

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v63
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v63
Deposition date deposition_date2021-08-19
Structure title titleStructure of dimeric uPAR at low pH
Keywords keywordsGPI-anchored protein, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.60
Radius of gyration Rg (electron density) rg_electron28.67
Forward intensity I(0) i035895400.00
Molecular weight molecular_weight41094.0 kDa
Excluded volume excluded_volume49349 ų
Envelope volume envelope_volume81653 ų
Hydration-shell volume shell_volume25132 ų
Envelope diameter envelope_diameter89.1
Shell Rg shell_rg34.74
Envelope Rg envelope_rg26.59
Shape Rg shape_rg28.65
Total Rg total_rg29.38
Total atoms total_atoms2833
Residues n_residues371
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 dmax90.7
Rg (real space) rg_real29.50
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real3.5900e+07
I(0) uncertainty (real space) i0_real_error4.9660e+05
Rg (reciprocal space) rg_reciprocal29.55
I(0) (reciprocal space) i0_reciprocal35900000.0000
Solution quality estimate total_estimate0.8359
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.7
Skewness Skewness skewness0.004
Kurtosis Kurtosis kurtosis-0.855
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1281000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.958; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)