1l4z

X-RAY CRYSTAL STRUCTURE OF THE COMPLEX OF MICROPLASMINOGEN WITH ALPHA DOMAIN OF STREPTOKINASE IN THE PRESENCE CADMIUM IONS

Method: X-RAY DIFFRACTION Dmax: 75.0 Å Quality: GOOD

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

Plasminogen

Homo sapiens

UniProt P00747

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 A; UniProt 563–810 Fragment:Catalytic domain, Residues 544-791 Mutation:S741A Streptokinase × 1 (P00779) CD CADMIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;Na acetate, cadmium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 563–810 Fragment:Catalytic domain, Residues 544-791 Mutation:S741A Streptokinase × 2 (P00779) CD CADMIUM ION × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;Na acetate, cadmium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.262

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.

46 other PDB entries and 75 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLMN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–248; UniProt 563–810

Streptokinase

Streptococcus dysgalactiae subsp. equisimilis

UniProt P00779

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 B; UniProt 1–147 Fragment:N terminal alpha domain, Residues 0-147 Mutation:Q5E, W6A Plasminogen × 1 (P00747) CD CADMIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;Na acetate, cadmium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–147 Fragment:N terminal alpha domain, Residues 0-147 Mutation:Q5E, W6A Plasminogen × 2 (P00747) CD CADMIUM ION × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;Na acetate, cadmium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.80 Å R-free 0.262

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.

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

View Construct and Data Evidence
UniProt name STRP_STREQ
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–136; UniProt 1–147

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 1l4z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1l4z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1l4z
Deposition date deposition_date2002-03-06
Structure title titleX-RAY CRYSTAL STRUCTURE OF THE COMPLEX OF MICROPLASMINOGEN WITH ALPHA DOMAIN OF STREPTOKINASE IN THE PRESENCE CADMIUM IONS
Keywords keywordsplasminogen, streptokinase, protein complex, HYDROLASE-BLOOD CLOTTING COMPLEX; HYDROLASE/BLOOD CLOTTING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.33
Radius of gyration Rg (electron density) rg_electron22.62
Forward intensity I(0) i030875900.00
Molecular weight molecular_weight41648.0 kDa
Excluded volume excluded_volume51560 ų
Envelope volume envelope_volume62724 ų
Hydration-shell volume shell_volume23348 ų
Envelope diameter envelope_diameter77.1
Shell Rg shell_rg29.25
Envelope Rg envelope_rg22.85
Shape Rg shape_rg22.64
Total Rg total_rg23.35
Total atoms total_atoms2888
Residues n_residues373
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 dmax75.0
Rg (real space) rg_real23.31
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real3.0880e+07
I(0) uncertainty (real space) i0_real_error4.1590e+05
Rg (reciprocal space) rg_reciprocal23.31
I(0) (reciprocal space) i0_reciprocal30880000.0000
Solution quality estimate total_estimate0.8990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.328
Kurtosis Kurtosis kurtosis-0.392
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9009000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1l4za_
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
Domain ID domain_idd1l4zb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.5 — Staphylokinase/streptokinase
Family Family familyd.15.5.1 — Staphylokinase/streptokinase

CATH v4.4 (3 domains)

Domain ID domain_id1l4zA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1l4zA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1l4zB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily180

8. Citations (1)

9. Files and Curves (10)