5zlz

Structure of tPA and PAI-1

Method: X-RAY DIFFRACTION Dmax: 104.6 Å Quality: GOOD

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

Plasminogen activator inhibitor 1

Homo sapiens

UniProt P05121

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 29–402 Mutation:N173H, K177T, Q342L, M377I Tissue-type plasminogen activator × 1 (P00750) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;4-8% PEG 3350, 20 mM bis-Tris-HCl pH 7.0 Resolution 3.58 Å R-free 0.312

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.

28 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAI1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain I; PDBConstruct 1–374; UniProt 29–402

Tissue-type plasminogen activator

Homo sapiens

UniProt P00750

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 311–561 Mutation:C430A, F458E, N483Q, S513A Plasminogen activator inhibitor 1 × 1 (P05121) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;4-8% PEG 3350, 20 mM bis-Tris-HCl pH 7.0 Resolution 3.58 Å R-free 0.312

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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–251; UniProt 311–561

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 5zlz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5zlz
Deposition date deposition_date2018-03-31
Structure title titleStructure of tPA and PAI-1
Keywords keywordsPAI-1, fibrinolysis, PAItrap2, HYDROLASE INHIBITOR-HYDROLASE complex; HYDROLASE INHIBITOR/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.04
Radius of gyration Rg (electron density) rg_electron30.72
Forward intensity I(0) i076516900.00
Molecular weight molecular_weight69492.0 kDa
Excluded volume excluded_volume87052 ų
Envelope volume envelope_volume107770 ų
Hydration-shell volume shell_volume31131 ų
Envelope diameter envelope_diameter111.4
Shell Rg shell_rg35.72
Envelope Rg envelope_rg31.01
Shape Rg shape_rg30.71
Total Rg total_rg31.21
Total atoms total_atoms4891
Residues n_residues599
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 dmax104.6
Rg (real space) rg_real31.36
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real7.6520e+07
I(0) uncertainty (real space) i0_real_error1.2300e+06
Rg (reciprocal space) rg_reciprocal31.23
I(0) (reciprocal space) i0_reciprocal76510000.0000
Solution quality estimate total_estimate0.8061
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.7
Skewness Skewness skewness0.568
Kurtosis Kurtosis kurtosis-0.351
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40640000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.680; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.705; Smooth: 0.731

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id5zlzE02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id5zlzI01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology497 — Antithrombin; Chain I, domain 2
Homologous superfamily homologous superfamily10 — Antithrombin, subunit I, domain 2
Domain ID domain_id5zlzI02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology39 — Alpha-1-antitrypsin; domain 1
Homologous superfamily homologous superfamily10 — Alpha-1-antitrypsin, domain 1

8. Citations (1)

9. Files and Curves (10)