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PDBsum entry 3qt4

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protein ligands links
Hydrolase PDB id
3qt4

 

 

 

 

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Contents
Protein chain
304 a.a.
Ligands
PO4 ×10
PG4 ×7
PG6 ×2
Waters ×262
PDB id:
3qt4
Name: Hydrolase
Title: Structure of digestive procathepsin l 3 of tenebrio molitor larval midgut
Structure: Cathepsin-l-like midgut cysteine proteinase. Chain: a. Engineered: yes. Mutation: yes
Source: Tenebrio molitor. Yellow mealworm beetle. Organism_taxid: 7067. Gene: pcal3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.11Å     R-factor:   0.160     R-free:   0.201
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:
22-Feb-11     Release date:   22-Feb-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q7YXL2  (Q7YXL2_TENMO) -  Cathepsin-L-like midgut cysteine proteinase from Tenebrio molitor
Seq:
Struc:
330 a.a.
304 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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