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PDBsum entry 2dc7

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protein ligands links
Hydrolase PDB id
2dc7

 

 

 

 

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Contents
Protein chain
251 a.a. *
Ligands
PO4
042
GOL
Waters ×227
* Residue conservation analysis
PDB id:
2dc7
Name: Hydrolase
Title: X-ray crystal structure analysis of bovine spleen cathepsin b-ca042 complex
Structure: Cathepsin b. Chain: a. Ec: 3.4.22.1
Source: Bos taurus. Cattle. Organism_taxid: 9913. Tissue: spleen
Resolution:
1.94Å     R-factor:   0.187     R-free:   0.214
Authors: D.Watanabe
Key ref: D.Watanabe et al. Quantitative estimation of each active subsite of cathepsin b for the inhibitory activity, Based on the inhibitory activitybinding mode relationship of a series of epoxysuccinyl inhibitors by x-Ray crystal structure analyses of the complexes. To be published, .
Date:
31-Dec-05     Release date:   24-Jan-06    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07688  (CATB_BOVIN) -  Cathepsin B from Bos taurus
Seq:
Struc:
335 a.a.
251 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.22.1  - cathepsin B.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.

 

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