PDBsum entry 1l4z

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protein metals Protein-protein interface(s) links
Hydrolase/blood clotting PDB id
Protein chains
248 a.a. *
125 a.a. *
_CD ×6
Waters ×70
* Residue conservation analysis
PDB id:
Name: Hydrolase/blood clotting
Title: X-ray crystal structure of the complex of microplasminogen with alpha domain of streptokinase in the presence cadmium ions
Structure: Plasminogen. Chain: a. Fragment: catalytic domain, residues 544-791. Engineered: yes. Mutation: yes. Streptokinase. Chain: b. Fragment: n terminal alpha domain, residues 0-147. Engineered: yes.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Streptococcus dysgalactiae subsp. Equisimilis. Organism_taxid: 119602. Strain: subsp. Equisimilis.
Biol. unit: Tetramer (from PQS)
2.80Å     R-factor:   0.220     R-free:   0.262
Authors: N.Wakeham,S.Terzyan,P.Zhai,J.A.Loy,J.Tang,X.C.Zhang
Key ref: N.Wakeham et al. (2002). Effects of deletion of streptokinase residues 48-59 on plasminogen activation. Protein Eng, 15, 753-761. PubMed id: 12456874
06-Mar-02     Release date:   11-Dec-02    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00747  (PLMN_HUMAN) -  Plasminogen
810 a.a.
248 a.a.*
Protein chain
Pfam   ArchSchema ?
P00779  (STRP_STREQ) -  Streptokinase C
440 a.a.
125 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.  - Plasmin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     catalytic activity     2 terms  


Protein Eng 15:753-761 (2002)
PubMed id: 12456874  
Effects of deletion of streptokinase residues 48-59 on plasminogen activation.
N.Wakeham, S.Terzyan, P.Zhai, J.A.Loy, J.Tang, X.C.Zhang.
Streptokinase (SK) is a thrombolytic agent widely used for the clinical treatment of clotting disorders such as heart attack. The treatment is based on the ability of SK to bind plasminogen (Pg) or plasmin (Pm), forming complexes that proteolytically activate other Pg molecules to Pm, which carries out fibrinolysis. SK contains three major domains. The N-terminal domain, SKalpha, provides the complex with substrate recognition towards Pg. SKalpha contains a unique mobile loop, residues 45-70, absent in the corresponding domains of other bacterial Pg activators. To study the roles of this loop, we deleted 12 residues in this loop in both full-length SK and the SKalpha fragment. Kinetic data indicate that this loop participates in the recognition of substrate Pg, but does not function in the active site formation in the activator complex. Two crystal structures of the deletion mutant of SKalpha (SKalpha(delta)) complexed with the protease domain of Pg were determined. While the structure of SKalpha(delta) is essentially the same as this domain in full-length SK, the mode of SK-Pg interaction was however different from a previously observed structure. Even though mutagenesis studies indicated that the current complex represents a minor interacting form in solution, the binding to SKalpha(delta) triggered similar conformational changes in the Pg active site in both crystal forms.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19473980 A.C.Tharp, M.Laha, P.Panizzi, M.W.Thompson, P.Fuentes-Prior, and P.E.Bock (2009).
Plasminogen substrate recognition by the streptokinase-plasminogen catalytic complex is facilitated by Arg253, Lys256, and Lys257 in the streptokinase beta-domain and kringle 5 of the substrate.
  J Biol Chem, 284, 19511-19521.  
19801674 R.Aneja, M.Datt, B.Singh, S.Kumar, and G.Sahni (2009).
Identification of a new exosite involved in catalytic turnover by the streptokinase-plasmin activator complex during human plasminogen activation.
  J Biol Chem, 284, 32642-32650.  
17111203 A.Kunamneni, T.T.Abdelghani, and P.Ellaiah (2007).
Streptokinase--the drug of choice for thrombolytic therapy.
  J Thromb Thrombolysis, 23, 9.  
15623524 R.R.Bean, I.M.Verhamme, and P.E.Bock (2005).
Role of the streptokinase alpha-domain in the interactions of streptokinase with plasminogen and plasmin.
  J Biol Chem, 280, 7504-7510.  
15211511 S.Terzyan, N.Wakeham, P.Zhai, K.Rodgers, and X.C.Zhang (2004).
Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain.
  Proteins, 56, 277-284.
PDB code: 1rjx
14732928 R.L.Rich, and D.G.Myszka (2003).
A survey of the year 2002 commercial optical biosensor literature.
  J Mol Recognit, 16, 351-382.  
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