5zc5

uPA-NU-09F

Method: X-RAY DIFFRACTION Dmax: 58.7 Å Quality: REASONABLE

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

Urokinase-type plasminogen activator chain B

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 179–431 Mutation:C122A, N145Q 09I 3-azanyl-5-(azepan-1-yl)-N-carbamimidoyl-6-(4-fluoranyl-1-benzofuran-2-yl)pyrazine-2-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;50mM sodium citrate pH 4.6, 1.95M (NH4)2SO4, 0.03% NaN3, 5% PEG 400 Resolution 1.90 Å R-free 0.235

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 1–253; 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 5zc5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5zc5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5zc5
Deposition date deposition_date2018-02-15
Structure title titleuPA-NU-09F
Keywords keywordsuPA, Inhibitor, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.07
Radius of gyration Rg (electron density) rg_electron17.04
Forward intensity I(0) i026323300.00
Molecular weight molecular_weight26018.0 kDa
Excluded volume excluded_volume24986 ų
Envelope volume envelope_volume38975 ų
Hydration-shell volume shell_volume18596 ų
Envelope diameter envelope_diameter60.3
Shell Rg shell_rg23.84
Envelope Rg envelope_rg17.47
Shape Rg shape_rg17.03
Total Rg total_rg17.81
Total atoms total_atoms1963
Residues n_residues226
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 dmax58.7
Rg (real space) rg_real17.95
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real2.6320e+07
I(0) uncertainty (real space) i0_real_error2.8980e+05
Rg (reciprocal space) rg_reciprocal17.96
I(0) (reciprocal space) i0_reciprocal26320000.0000
Solution quality estimate total_estimate0.7444
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.196
Kurtosis Kurtosis kurtosis-0.324
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7534000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.823; Stabil: 1.000; Sysdev: 0.408; Positv: 1.000; Valcen: 0.992; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5zc5u_
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 (1 domains)

Domain ID domain_id5zc5U02
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)