1urk

SOLUTION STRUCTURE OF THE AMINO TERMINAL FRAGMENT OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR

Method: SOLUTION NMR Dmax: 93.8 Å Quality: REASONABLE

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

PLASMINOGEN ACTIVATOR

Homo sapiens

UniProt P00749

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 26–155 Not recorded FUC alpha-L-fucopyranose × 1 SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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.

147 other PDB entries and 165 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UROK_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–130; UniProt 26–155

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 1urk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1urk
Deposition date deposition_date1994-01-10
Structure title titleSOLUTION STRUCTURE OF THE AMINO TERMINAL FRAGMENT OF UROKINASE-TYPE PLASMINOGEN ACTIVATOR
Keywords keywordsPLASMINOGEN ACTIVATION; PLASMINOGEN ACTIVATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier22.60
Radius of gyration Rg (electron density) rg_electron22.43
Forward intensity I(0) i0854737000.00
Molecular weight molecular_weight222750.0 kDa
Excluded volume excluded_volume270260 ų
Envelope volume envelope_volume134130 ų
Hydration-shell volume shell_volume39235 ų
Envelope diameter envelope_diameter99.2
Shell Rg shell_rg36.21
Envelope Rg envelope_rg28.18
Shape Rg shape_rg22.44
Total Rg total_rg22.96
Total atoms total_atoms15525
Residues n_residues1950
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 dmax93.8
Rg (real space) rg_real22.69
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real8.5470e+08
I(0) uncertainty (real space) i0_real_error1.3510e+07
Rg (reciprocal space) rg_reciprocal22.67
I(0) (reciprocal space) i0_reciprocal854700000.0000
Solution quality estimate total_estimate0.7408
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.566
Kurtosis Kurtosis kurtosis0.181
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha79950000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.354; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.565; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1urka1
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.1 — EGF-type module
Domain ID domain_idd1urka2
Class classg — Small proteins
Fold Fold foldg.14 — Kringle-like
Superfamily Superfamily superfamilyg.14.1 — Kringle-like
Family Family familyg.14.1.1 — Kringle modules

CATH v4.4 (2 domains)

Domain ID domain_id1urkA01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin
Domain ID domain_id1urkA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4

8. Citations (1)

9. Files and Curves (10)