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PDBsum entry 3js5

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protein ligands metals links
Hydrolase PDB id
3js5

 

 

 

 

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Contents
Protein chain
156 a.a. *
Ligands
EPE
Metals
_NA
Waters ×164
* Residue conservation analysis
PDB id:
3js5
Name: Hydrolase
Title: Crystal structure of protein tyrosine phosphatase from entamoeba histolytica with hepes in the active site. High resolution, alternative crystal form with 1 molecule in asymmetric unit
Structure: Protein tyrosine phosphatase. Chain: a. Engineered: yes
Source: Entamoeba histolytica. Organism_taxid: 294381. Strain: hm-1:imss. Gene: ehi_153650. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.94Å     R-factor:   0.169     R-free:   0.212
Authors: Seattle Structural Genomics Center For Infectious Disease (Ssgcid)
Key ref: A.S.Linford et al. (2014). Crystal structure and putative substrate identification for the Entamoeba histolytica low molecular weight tyrosine phosphatase. Mol Biochem Parasitol, 193, 33-44. PubMed id: 24548880 DOI: 10.1016/j.molbiopara.2014.01.003
Date:
09-Sep-09     Release date:   22-Sep-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
C4LSE7  (C4LSE7_ENTHI) -  acid phosphatase from Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Seq:
Struc:
157 a.a.
156 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.2  - acid phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a phosphate monoester + H2O = an alcohol + phosphate
phosphate monoester
+ H2O
= alcohol
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.molbiopara.2014.01.003 Mol Biochem Parasitol 193:33-44 (2014)
PubMed id: 24548880  
 
 
Crystal structure and putative substrate identification for the Entamoeba histolytica low molecular weight tyrosine phosphatase.
A.S.Linford, N.M.Jiang, T.E.Edwards, N.E.Sherman, W.C.Van Voorhis, L.J.Stewart, P.J.Myler, B.L.Staker, W.A.Petri.
 
  ABSTRACT  
 
No abstract given.

 

 

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