1bml

COMPLEX OF THE CATALYTIC DOMAIN OF HUMAN PLASMIN AND STREPTOKINASE

Method: X-RAY DIFFRACTION Dmax: 100.0 Å Quality: GOOD

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

PLASMIN

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 561–810 Chain B; UniProt 561–810 Fragment:CATALYTIC DOMAIN Mutation:S741A STREPTOKINASE × 2 (P00779) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.90 Å R-free 0.291
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 561–810 Fragment:CATALYTIC DOMAIN Mutation:S741A STREPTOKINASE × 1 (P00779) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.90 Å R-free 0.291
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 561–810 Fragment:CATALYTIC DOMAIN Mutation:S741A STREPTOKINASE × 1 (P00779) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.90 Å R-free 0.291

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 74 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 1–250; UniProt 561–810 Author chain B; PDBConstruct 1–250; UniProt 561–810

STREPTOKINASE

OrganismNot specified

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 38–399 Chain D; UniProt 38–399 Not recorded PLASMIN × 2 (P00747) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.90 Å R-free 0.291
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 38–399 Not recorded PLASMIN × 1 (P00747) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.90 Å R-free 0.291
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 38–399 Not recorded PLASMIN × 1 (P00747) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.90 Å R-free 0.291

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 9 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 C; PDBConstruct 1–361; UniProt 38–399 Author chain D; PDBConstruct 1–361; UniProt 38–399

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 1bml

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bml
Deposition date deposition_date1999-05-25
Structure title titleCOMPLEX OF THE CATALYTIC DOMAIN OF HUMAN PLASMIN AND STREPTOKINASE
Keywords keywordsHUMAN PLASMIN, STREPTOKINASE, 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_guinier34.15
Radius of gyration Rg (electron density) rg_electron33.38
Forward intensity I(0) i0252942000.00
Molecular weight molecular_weight126860.0 kDa
Excluded volume excluded_volume158650 ų
Envelope volume envelope_volume216670 ų
Hydration-shell volume shell_volume52629 ų
Envelope diameter envelope_diameter100.5
Shell Rg shell_rg41.73
Envelope Rg envelope_rg32.20
Shape Rg shape_rg33.38
Total Rg total_rg34.04
Total atoms total_atoms8940
Residues n_residues1136
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 dmax100.0
Rg (real space) rg_real33.91
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real2.5290e+08
I(0) uncertainty (real space) i0_real_error3.5540e+06
Rg (reciprocal space) rg_reciprocal34.06
I(0) (reciprocal space) i0_reciprocal253000000.0000
Solution quality estimate total_estimate0.8363
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.8
Skewness Skewness skewness-0.031
Kurtosis Kurtosis kurtosis-0.642
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44970000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.962; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd1bmla_
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_idd1bmlb_
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_idd1bmlc1
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
Domain ID domain_idd1bmlc2
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
Domain ID domain_idd1bmlc3
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
Domain ID domain_idd1bmld1
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
Domain ID domain_idd1bmld2
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
Domain ID domain_idd1bmld3
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 (10 domains)

Domain ID domain_id1bmlA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1bmlA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1bmlB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1bmlB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1bmlC01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily180
Domain ID domain_id1bmlC02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily180
Domain ID domain_id1bmlC03
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily150
Domain ID domain_id1bmlD01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily180
Domain ID domain_id1bmlD02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily180
Domain ID domain_id1bmlD03
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily150

8. Citations (1)

9. Files and Curves (10)