1o5c

Dissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an Artificial Ala190 Protease (Ala190 uPA)

Method: X-RAY DIFFRACTION Dmax: 58.5 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 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 Mutation:N145A/S190A CR9 2-{5-[AMINO(IMINIO)METHYL]-6-FLUORO-1H-BENZIMIDAZOL-2-YL}-6-[(2-METHYLCYCLOHEXYL)OXY]BENZENOLATE × 1 CIT CITRIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;298 K;2-propanol, PEG 4000, pH 6.5, vapor diffusion at 298 K, pH 6.5, pH 6.50 Resolution 1.63 Å R-free 0.219

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 1o5c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1o5c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1o5c
Deposition date deposition_date2003-09-09
Structure title titleDissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an Artificial Ala190 Protease (Ala190 uPA)
Keywords keywords;Ala190 uPA, S1 site, selectivity, conserved water displacement hydrogen bond deficit, trypsin, thrombin, hepsin, factor VIIa, BLOOD CLOTTING, hydrolase ;; BLOOD CLOTTING, hydrolase
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.50
Radius of gyration Rg (electron density) rg_electron17.32
Forward intensity I(0) i015830300.00
Molecular weight molecular_weight29448.0 kDa
Excluded volume excluded_volume36611 ų
Envelope volume envelope_volume40622 ų
Hydration-shell volume shell_volume19097 ų
Envelope diameter envelope_diameter58.0
Shell Rg shell_rg24.18
Envelope Rg envelope_rg17.69
Shape Rg shape_rg17.30
Total Rg total_rg18.36
Total atoms total_atoms4072
Residues n_residues236
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 dmax58.5
Rg (real space) rg_real18.56
Rg uncertainty (real space) rg_real_error0.11
I(0) (real space) i0_real1.5430e+07
I(0) uncertainty (real space) i0_real_error1.4810e+05
Rg (reciprocal space) rg_reciprocal18.40
I(0) (reciprocal space) i0_reciprocal15830000.0000
Solution quality estimate total_estimate0.6977
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary23.2
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.227
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha8.6600
Highest regularization parameter α highest_alpha4568000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 0.930; Sysdev: 0.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.690

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_idd1o5c.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_id1o5cB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1o5cB02
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)