2vnt

Urokinase-Type Plasminogen Activator Inhibitor Complex with a 1-(7- SULPHOAMIDOISOQUINOLINYL)GUANIDINE

Method: X-RAY DIFFRACTION Dmax: 122.5 Å Quality: EXCELLENT

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 A; UniProt 156–431 Fragment:CATALYTIC DOMAIN, RESIDUES 156-431 QGG 1-({4-CHLORO-1-[(DIAMINOMETHYLIDENE)AMINO]ISOQUINOLIN-7-YL}SULFONYL)-D-PROLINE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å R-free 0.295
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 156–431 Fragment:CATALYTIC DOMAIN, RESIDUES 156-431 QGG 1-({4-CHLORO-1-[(DIAMINOMETHYLIDENE)AMINO]ISOQUINOLIN-7-YL}SULFONYL)-D-PROLINE × 1 SO4 SULFATE ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å R-free 0.295
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 156–431 Fragment:CATALYTIC DOMAIN, RESIDUES 156-431 QGG 1-({4-CHLORO-1-[(DIAMINOMETHYLIDENE)AMINO]ISOQUINOLIN-7-YL}SULFONYL)-D-PROLINE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å R-free 0.295
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 156–431 Fragment:CATALYTIC DOMAIN, RESIDUES 156-431 QGG 1-({4-CHLORO-1-[(DIAMINOMETHYLIDENE)AMINO]ISOQUINOLIN-7-YL}SULFONYL)-D-PROLINE × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å R-free 0.295
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 156–431 Fragment:CATALYTIC DOMAIN, RESIDUES 156-431 QGG 1-({4-CHLORO-1-[(DIAMINOMETHYLIDENE)AMINO]ISOQUINOLIN-7-YL}SULFONYL)-D-PROLINE × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å R-free 0.295
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 156–431 Fragment:CATALYTIC DOMAIN, RESIDUES 156-431 QGG 1-({4-CHLORO-1-[(DIAMINOMETHYLIDENE)AMINO]ISOQUINOLIN-7-YL}SULFONYL)-D-PROLINE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å R-free 0.295

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 160 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 1–273; UniProt 156–431 Author chain B; PDBConstruct 1–276; UniProt 156–431 Author chain C; PDBConstruct 1–276; UniProt 156–431 Author chain D; PDBConstruct 1–276; UniProt 156–431 Author chain E; PDBConstruct 1–276; UniProt 156–431 Author chain F; PDBConstruct 1–276; UniProt 156–431

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 2vnt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2vnt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2vnt
Deposition date deposition_date2008-02-07
Structure title titleUrokinase-Type Plasminogen Activator Inhibitor Complex with a 1-(7- SULPHOAMIDOISOQUINOLINYL)GUANIDINE
Keywords keywordsUPA, INHIBITOR COMPLEX, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.90
Radius of gyration Rg (electron density) rg_electron38.53
Forward intensity I(0) i0505169000.00
Molecular weight molecular_weight177630.0 kDa
Excluded volume excluded_volume219620 ų
Envelope volume envelope_volume282360 ų
Hydration-shell volume shell_volume59737 ų
Envelope diameter envelope_diameter126.4
Shell Rg shell_rg45.33
Envelope Rg envelope_rg38.33
Shape Rg shape_rg38.50
Total Rg total_rg38.98
Total atoms total_atoms12421
Residues n_residues1551
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 dmax122.5
Rg (real space) rg_real38.80
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real5.0520e+08
I(0) uncertainty (real space) i0_real_error8.4980e+06
Rg (reciprocal space) rg_reciprocal38.87
I(0) (reciprocal space) i0_reciprocal505200000.0000
Solution quality estimate total_estimate0.9056
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.8
Skewness Skewness skewness0.211
Kurtosis Kurtosis kurtosis-0.659
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha122000000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.924

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id2vntA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntC02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntD01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntD02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntE01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntE02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntF01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2vntF02
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)