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PDBsum entry 2xe4

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protein ligands metals links
Hydrolase/inhibitor PDB id
2xe4

 

 

 

 

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Contents
Protein chain
721 a.a. *
Ligands
FC0-ARG-VAL-RGL
GOL ×10
PGR ×48
PGO
PO4 ×3
Metals
_CL ×4
_NA ×2
Waters ×721
* Residue conservation analysis
PDB id:
2xe4
Name: Hydrolase/inhibitor
Title: Structure of oligopeptidase b from leishmania major
Structure: Oligopeptidase b. Chain: a. Synonym: family s9a-like protein, serine peptidase. Engineered: yes. Mutation: yes. Antipain. Chain: b
Source: Leishmania major. Organism_taxid: 5664. Strain: friedlin. Expressed in: escherichia coli. Expression_system_taxid: 469008. Actinobacteria. Organism_taxid: 1760
Resolution:
1.65Å     R-factor:   0.142     R-free:   0.178
Authors: K.Mcluskey,N.G.Paterson,N.D.Bland,J.C.Mottram,N.W.Isaacs
Key ref: K.McLuskey et al. (2010). Crystal structure of Leishmania major oligopeptidase B gives insight into the enzymatic properties of a trypanosomatid virulence factor. J Biol Chem, 285, 39249-39259. PubMed id: 20926390
Date:
11-May-10     Release date:   06-Oct-10    
PROCHECK
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 Headers
 References

Protein chain
Q4QHU7  (Q4QHU7_LEIMA) -  Prolyl endopeptidase from Leishmania major
Seq:
Struc:
 
Seq:
Struc:
731 a.a.
721 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: E.C.3.4.21.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: E.C.3.4.21.26  - prolyl oligopeptidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

 
J Biol Chem 285:39249-39259 (2010)
PubMed id: 20926390  
 
 
Crystal structure of Leishmania major oligopeptidase B gives insight into the enzymatic properties of a trypanosomatid virulence factor.
K.McLuskey, N.G.Paterson, N.D.Bland, N.W.Isaacs, J.C.Mottram.
 
  ABSTRACT  
 
No abstract given.

 

 

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