3u74

Crystal structure of stabilized human uPAR mutant

Method: X-RAY DIFFRACTION Dmax: 65.7 Å Quality: REASONABLE

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 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain U; UniProt 23–305 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;295 K;100 mM HEPES, pH 7.5, 2% (w/v) PEG400, 2 M ammonium sulfate, vapor diffusion, sitting drop, temperature 295.0K Resolution 2.39 Å R-free 0.252

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 U; PDBConstruct 1–283; UniProt 23–305

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 3u74

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3u74
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3u74
Deposition date deposition_date2011-10-13
Structure title titleCrystal structure of stabilized human uPAR mutant
Keywords keywordsglycosylation, HYDROLASE RECEPTOR; HYDROLASE RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.54
Radius of gyration Rg (electron density) rg_electron19.66
Forward intensity I(0) i019699100.00
Molecular weight molecular_weight29830.0 kDa
Excluded volume excluded_volume35749 ų
Envelope volume envelope_volume44376 ų
Hydration-shell volume shell_volume19019 ų
Envelope diameter envelope_diameter63.3
Shell Rg shell_rg25.68
Envelope Rg envelope_rg19.71
Shape Rg shape_rg19.66
Total Rg total_rg20.46
Total atoms total_atoms2059
Residues n_residues263
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 dmax65.7
Rg (real space) rg_real20.44
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real1.9700e+07
I(0) uncertainty (real space) i0_real_error2.5620e+05
Rg (reciprocal space) rg_reciprocal20.46
I(0) (reciprocal space) i0_reciprocal19700000.0000
Solution quality estimate total_estimate0.7077
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.7
Skewness Skewness skewness0.106
Kurtosis Kurtosis kurtosis-0.605
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2093000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 0.138; Positv: 1.000; Valcen: 1.000; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3u74u1
Class classg — Small proteins
Fold Fold foldg.7 — Snake toxin-like
Superfamily Superfamily superfamilyg.7.1 — Snake toxin-like
Family Family familyg.7.1.0 — automated matches
Domain ID domain_idd3u74u2
Class classg — Small proteins
Fold Fold foldg.7 — Snake toxin-like
Superfamily Superfamily superfamilyg.7.1 — Snake toxin-like
Family Family familyg.7.1.0 — automated matches
Domain ID domain_idd3u74u3
Class classg — Small proteins
Fold Fold foldg.7 — Snake toxin-like
Superfamily Superfamily superfamilyg.7.1 — Snake toxin-like
Family Family familyg.7.1.0 — automated matches

CATH v4.4 (3 domains)

Domain ID domain_id3u74U01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id3u74U02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id3u74U03
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59

8. Citations (1)

9. Files and Curves (10)