1c5y

STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR

Method: X-RAY DIFFRACTION Dmax: 59.5 Å Quality: GOOD

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

PROTEIN (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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 156–178 Chain B; UniProt 179–431 Fragment:SHORT CHAIN Fragment:CATALYTIC DOMAIN FLC CITRATE ANION × 3 ESP THIENO[2,3-B]PYRIDINE-2-CARBOXAMIDINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;LMW human uPA/A145 was concentrated to 10 mg/ml and incubated in 50 mM HEPES, 5.0 mM NaCl. pH 7.0, 5.0 mM thieno[2,3-b]pyridine-2-carboxamidine for 15 min on ice. The complex was crystallized by vapor diffusion in hanging drops containing equal volumes of protein-inhibitor solution (0.28 mM uPA/A145, 1.4 mM inhibitor and well solution (20 % 2-propanol, 20 % PEG 4K, 100 mM sodium citrate, pH 6.5) sealed over the well. Resolution 1.65 Å R-free 0.246

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–23; UniProt 156–178 Author chain B; PDBConstruct 1–253; UniProt 179–431

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 1c5y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c5y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c5y
Deposition date deposition_date1999-12-22
Structure title titleSTRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR
Keywords keywordsselective, S1 site inhibitor, structure-based drug design, urokinase, trypsin, thrombin, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.47
Radius of gyration Rg (electron density) rg_electron17.31
Forward intensity I(0) i016135300.00
Molecular weight molecular_weight29510.0 kDa
Excluded volume excluded_volume36571 ų
Envelope volume envelope_volume40982 ų
Hydration-shell volume shell_volume19198 ų
Envelope diameter envelope_diameter60.2
Shell Rg shell_rg24.24
Envelope Rg envelope_rg17.75
Shape Rg shape_rg17.30
Total Rg total_rg18.33
Total atoms total_atoms4073
Residues n_residues257
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 dmax59.5
Rg (real space) rg_real18.36
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real1.6140e+07
I(0) uncertainty (real space) i0_real_error1.8610e+05
Rg (reciprocal space) rg_reciprocal18.37
I(0) (reciprocal space) i0_reciprocal16140000.0000
Solution quality estimate total_estimate0.8035
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.169
Kurtosis Kurtosis kurtosis-0.331
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5274000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1c5y.1
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_id1c5yB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1c5yB02
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)