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PDBsum entry 3qj3

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3qj3

 

 

 

 

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Contents
Protein chains
319 a.a.
Ligands
ACT ×4
Waters ×530
PDB id:
3qj3
Name: Hydrolase
Title: Structure of digestive procathepsin l2 proteinase from tenebrio molitor larval midgut
Structure: Cathepsin l-like protein. Chain: a, b. Engineered: yes. Mutation: yes
Source: Tenebrio molitor. Yellow mealworm beetle. Organism_taxid: 7067. Gene: pcal2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.85Å     R-factor:   0.186     R-free:   0.231
Authors: D.Beton,C.R.Guzzo,W.R.Terra,C.S.Farah
Key ref: D.Beton et al. (2012). The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut. Insect Biochem Mol Biol, 42, 655-664. PubMed id: 22659439
Date:
28-Jan-11     Release date:   01-Feb-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q69G21  (Q69G21_TENMO) -  C1 family cathepsin L5 from Tenebrio molitor
Seq:
Struc:
336 a.a.
319 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.4.22.15  - cathepsin L.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.

 

 
Insect Biochem Mol Biol 42:655-664 (2012)
PubMed id: 22659439  
 
 
The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut.
D.Beton, C.R.Guzzo, A.F.Ribeiro, C.S.Farah, W.R.Terra.
 
  ABSTRACT  
 
No abstract given.

 

 

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