4dva

The crystal structure of human urokinase-type plasminogen activator catalytic domain

Method: X-RAY DIFFRACTION Dmax: 62.2 Å Quality: REASONABLE

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

Urokinase-type 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 U; UniProt 179–424 Fragment:catalytic domain Mutation:C122A, N145Q SO4 SULFATE ION × 2 P6G HEXAETHYLENE GLYCOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;298 K;2.0M ammonium sulfate, 50mM sodium citrate, 5% PEG400, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.94 Å R-free 0.244

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 U; PDBConstruct 1–246; UniProt 179–424

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 4dva

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4dva
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4dva
Deposition date deposition_date2012-02-23
Structure title titleThe crystal structure of human urokinase-type plasminogen activator catalytic domain
Keywords keywordsHydrolase, Plasminogen activation, Protease, Serine protease; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.43
Radius of gyration Rg (electron density) rg_electron17.17
Forward intensity I(0) i014750900.00
Molecular weight molecular_weight28157.0 kDa
Excluded volume excluded_volume34951 ų
Envelope volume envelope_volume39339 ų
Hydration-shell volume shell_volume18654 ų
Envelope diameter envelope_diameter60.3
Shell Rg shell_rg23.97
Envelope Rg envelope_rg17.60
Shape Rg shape_rg17.15
Total Rg total_rg18.26
Total atoms total_atoms1972
Residues n_residues227
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 dmax62.2
Rg (real space) rg_real18.32
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.4750e+07
I(0) uncertainty (real space) i0_real_error1.9010e+05
Rg (reciprocal space) rg_reciprocal18.34
I(0) (reciprocal space) i0_reciprocal14750000.0000
Solution quality estimate total_estimate0.6458
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.7
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.300
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4490000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.746; Stabil: 0.994; Sysdev: 0.391; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4dvau_
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id4dvaU01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id4dvaU02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (1)

9. Files and Curves (10)