1fv9

Crystal structure of human microurokinase in complex with 2-amino-5-hydroxy-benzimidazole

Method: X-RAY DIFFRACTION Dmax: 60.5 Å Quality: GOOD

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

UROKINASE

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 179–423 Fragment:B CHAIN (16-243) Mutation:C122A, N145Q SO4 SULFATE ION × 1 172 2-AMINO-5-HYDROXY-BENZIMIDAZOLE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.15M LiSo4, 20% PEG 4000, succinate buffer, VAPOR DIFFUSION, HANGING DROP, temperature 18K Resolution 3.00 Å

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 1–245; UniProt 179–423

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 1fv9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1fv9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1fv9
Deposition date deposition_date2000-09-19
Structure title titleCrystal structure of human microurokinase in complex with 2-amino-5-hydroxy-benzimidazole
Keywords keywordsPlasminogen activation, 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_guinier18.32
Radius of gyration Rg (electron density) rg_electron17.17
Forward intensity I(0) i014441900.00
Molecular weight molecular_weight27804.0 kDa
Excluded volume excluded_volume34462 ų
Envelope volume envelope_volume38836 ų
Hydration-shell volume shell_volume18501 ų
Envelope diameter envelope_diameter60.6
Shell Rg shell_rg23.86
Envelope Rg envelope_rg17.56
Shape Rg shape_rg17.16
Total Rg total_rg18.17
Total atoms total_atoms1949
Residues n_residues245
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 dmax60.5
Rg (real space) rg_real18.21
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real1.4440e+07
I(0) uncertainty (real space) i0_real_error1.7150e+05
Rg (reciprocal space) rg_reciprocal18.23
I(0) (reciprocal space) i0_reciprocal14440000.0000
Solution quality estimate total_estimate0.8741
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.7
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.313
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3982000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1fv9a_
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_id1fv9A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1fv9A02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (2)

9. Files and Curves (10)