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PDBsum entry 1f2s
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protein metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
1f2s

 

 

 

 

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Contents
Protein chains
223 a.a. *
28 a.a. *
Metals
_CA
Waters ×207
* Residue conservation analysis
PDB id:
1f2s
Name: Hydrolase/hydrolase inhibitor
Title: Crystal structure of the complex formed between bovine beta-trypsin and mcti-a, a trypsin inhibitor of squash family at 1.8 a resolution
Structure: Trypsin. Chain: e. Trypsin inhibitor a. Chain: i
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreatic. Other_details: pancreatic. Momordica charantia. Balsam pear. Organism_taxid: 3673. Other_details: seed
Biol. unit: Dimer (from PQS)
Resolution:
1.79Å     R-factor:   0.177     R-free:   0.226
Authors: Y.Zhu,Q.Huang,M.Qian,Y.Jia,Y.Tang
Key ref: Y.Zhu et al. (1999). Crystal structure of the complex formed between bovine beta-trypsin and MCTI-A, a trypsin inhibitor of squash family, at 1.8-A resolution. J Protein Chem, 18, 505-509. PubMed id: 10524768
Date:
29-May-00     Release date:   05-Jun-00    
Supersedes: 1mcu
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00760  (TRY1_BOVIN) -  Serine protease 1 from Bos taurus
Seq:
Struc: 		246 a.a.
223 a.a.
Protein chain
Pfam   ArchSchema ?
P10295  (ITR2_MOMCH) -  Trypsin inhibitor 2 from Momordica charantia
Seq:
Struc: 		28 a.a.
28 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain E: E.C.3.4.21.4  - trypsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

 

 
J Protein Chem 18:505-509 (1999)
PubMed id: 10524768  
 
 
Crystal structure of the complex formed between bovine beta-trypsin and MCTI-A, a trypsin inhibitor of squash family, at 1.8-A resolution.
Y.Zhu, Q.Huang, M.Qian, Y.Jia, Y.Tang.
 
  ABSTRACT  
 
The stoichiometric complex formed between bovine beta-trypsin and Momordica charantia, Linn. Cucurbitaceae trypsin inhibitor A (MCTI-A) was crystallized and its X-ray crystal structure was refined to a final R value of 0.179 using data of 7.0- to 1.8-A resolution. Combination with results on the complex of MCTI-A with porcine trypsin gives the sequence of MCTI-A definitely, of which 13 residues are conserved compared with other squash family trypsin inhibitors. Its spatial structure and the conformation of its primary binding segment from Cys3I (P3) to Glu7I (P3'), which contains a reactive scissile bond Arg5I C-Ile6I N, were found to be very similar to the other squash family proteinase inhibitors.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19640842 R.Bao, C.Z.Zhou, C.Jiang, S.X.Lin, C.W.Chi, and Y.Chen (2009).
The ternary structure of the double-headed arrowhead protease inhibitor API-A complexed with two trypsins reveals a novel reactive site conformation.
  J Biol Chem, 284, 26676-26684.  
19077275 A.Heitz, O.Avrutina, D.Le-Nguyen, U.Diederichsen, J.F.Hernandez, J.Gracy, H.Kolmar, and L.Chiche (2008).
Knottin cyclization: Impact on Structure and Dynamics.
  BMC Struct Biol, 8, 54.  
15578663 O.Guvench, D.J.Price, and C.L.Brooks (2005).
Receptor rigidity and ligand mobility in trypsin-ligand complexes.
  Proteins, 58, 407-417.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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