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PDBsum entry 1r8o

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protein Protein-protein interface(s) links
Hydrolase inhibitor PDB id
1r8o

 

 

 

 

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Contents
Protein chains
96 a.a. *
71 a.a. *
Waters ×182
* Residue conservation analysis
PDB id:
1r8o
Name: Hydrolase inhibitor
Title: Crystal structure of an unusual kunitz-type trypsin inhibitor from copaifera langsdorffii seeds
Structure: Kunitz trypsin inhibitor. Chain: a. Fragment: residues 1-96. Synonym: sti. Kunitz trypsin inhibitor. Chain: b. Fragment: residues 97-167. Synonym: sti
Source: Copaifera langsdorffii. Organism_taxid: 280048. Organism_taxid: 280048
Biol. unit: Dimer (from PQS)
Resolution:
1.83Å     R-factor:   0.170     R-free:   0.212
Authors: S.Krauchenco,R.A.P.Nagem,J.A.Da Silva,S.Marangoni,I.Polikarpov
Key ref: S.Krauchenco et al. (2004). Three-dimensional structure of an unusual Kunitz (STI) type trypsin inhibitor from Copaifera langsdorffii. Biochimie, 86, 167-172. PubMed id: 15134830 DOI: 10.1016/j.biochi.2004.03.004
Date:
27-Oct-03     Release date:   25-May-04    
PROCHECK
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 Headers
 References

Protein chain
P84144  (P84144_COPLA) - 
Protein chain
P84145  (P84145_COPLA) - 
Key:    Secondary structure

 

 
DOI no: 10.1016/j.biochi.2004.03.004 Biochimie 86:167-172 (2004)
PubMed id: 15134830  
 
 
Three-dimensional structure of an unusual Kunitz (STI) type trypsin inhibitor from Copaifera langsdorffii.
S.Krauchenco, R.A.Nagem, J.A.da Silva, S.Marangoni, I.Polikarpov.
 
  ABSTRACT  
 
The crystallographic structure of a novel trypsin inhibitor (CTI) from Copaifera langsdorffii is reported. The structure was solved by MIRAS procedure and refined to a crystallographic residual of 17.3% (R(free) = 20.3%) at 1.8 A resolution. Two isomorphous derivatives were obtained by quick cryo-soaking approach. CTI is the first structure of a member of Kunitz (STI) family formed by two noncovalently bound polypeptide chains and only one disulfide bridge. A standard Kunitz-type inhibitor has a single polypeptide chain and two disulfide bridges. Structural features granting CTI high inhibitory activity are discussed.
 

 

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