1BML Blood Clotting Kinase date May 25, 1999
title Complex Of The Catalytic Domain Of Human Plasmin And Streptokinase
authors X.Wang, X.Lin, J.A.Loy, J.Tang, X.C.Zhang
compound source
Molecule: Plasmin
Chain: A, B
Fragment: Catalytic Domain
Ec: 3.4.21.7
Engineered: Yes
Mutation: S741a
 Organism_scientific: Homo Sapiens
Organism_common: Human
Expression_system: Escherichia Coli
Expression_system_common: Bacteria
Expression_system_strain: Bl21
Expression_system_vector: Pet11

Molecule: Streptokinase
Chain: C, D
Organism_scientific: Streptococcus Equisimilis
Organism_common: Bacteria
symmetry Space Group: P 1 21 1
R_factor 0.201
crystal
cell
length a length b length c angle alpha angle beta angle gamma
80.030 125.050 86.790 90.00 105.41 90.00
method X-Ray Diffractionresolution 2.90 Å
ligand
enzyme Hydrolase E.C.3.4.21.7
related structures by homologous chain: 1L4Z
similarity Plasminogen subfamily. Belongs to peptidase family s1. Contains 5 kringle domains. Contains 1 pan domain.[trypsin]
catalytic activ. Converts fibrin into soluble products. Preferential cleavage higher selectivity than trypsin.
post-translat. modifications O-linked glycans consist of gal-galnac disaccharide modified with up to 2 sialic acid residues (microheterogeneity). In the presence of the inhibitor, the activation involves only cleavage after arg-580, yielding two chains held together by two disulfide bonds. N-linked glycan contains n-acetyllactosamine and sialic acid. In the absence of the inhibitor, the activation involves addditionally the removal of the activation peptide.
tissue Present in plasma and many other extracellular fluids. It is synthesized in the kidney.
enzyme regulation Activated with catalytic amounts of streptokinase. Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin.
gene PLG (H. sapiens)
function It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as c1 and c5. Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation; in ovulation it weakens the walls of the graafian follicle. Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo. It cleaves fibrin, fibronectin, thrombospondin, laminin and von willebrand factor.
Gene
Ontology 		chain A: GO:0003809, GO:0004252, GO:0004263, GO:0004283, GO:0004295, GO:0005509, GO:0006508, GO:0007596, GO:0008285, GO:0016787, GO:0030195, GO:0050874
chain B: GO:0003809, GO:0004252, GO:0004263, GO:0004283, GO:0004295, GO:0005509, GO:0006508, GO:0007596, GO:0008285, GO:0016787, GO:0030195, GO:0050874
disease Conjunctivitis,ligneous
Plasminogen Tochigi disease
Plasminogen deficiency,types I and II
Thrombophilia,dysplasminogenemic
Defects in plg are a cause of thrombophilia [mim. 188050]; a form of recurrent thrombosis.
Primary referenceCrystal structure of the catalytic domain of human plasmin complexed with streptokinase., Wang X, Lin X, Loy JA, Tang J, Zhang XC, Science 1998 Sep 11;281(5383):1662-5. PMID:9733510
Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (207 Kb) [Save to disk]
  • Biological Unit Coordinates (1bml.pdb1.gz) 169 Kb
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        - Domain d1bmla_, region A [Jmol] [rasmolscript] [script source]
        - Domain d1bmlb_, region B [Jmol] [rasmolscript] [script source]
        - Domain d1bmlc1, region C:12-148 [Jmol] [rasmolscript] [script source]
        - Domain d1bmlc2, region C:149-284 [Jmol] [rasmolscript] [script source]
        - Domain d1bmlc3, region C:285-372 [Jmol] [rasmolscript] [script source]
        - Domain d1bmld1, region D:12-148 [Jmol] [rasmolscript] [script source]
        - Domain d1bmld2, region D:149-284 [Jmol] [rasmolscript] [script source]
        - Domain d1bmld3, region D:285-372 [Jmol] [rasmolscript] [script source]
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