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PDBsum entry 3ujc

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protein ligands links
Transferase PDB id
3ujc

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
258 a.a.
Ligands
_PC
Waters ×498
PDB id:
3ujc
Name: Transferase
Title: Phosphoethanolamine methyltransferase mutant (h132a) from plasmodium falciparum in complex with phosphocholine
Structure: Phosphoethanolamine n-methyltransferase. Chain: a. Engineered: yes
Source: Plasmodium falciparum. Organism_taxid: 5833. Gene: pmt. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.19Å     R-factor:   0.146     R-free:   0.167
Authors: S.G.Lee,Y.Kim,T.D.Alpert,A.Nagata,J.M.Jez
Key ref: S.G.Lee et al. (2012). Structure and reaction mechanism of phosphoethanolamine methyltransferase from the malaria parasite Plasmodium falciparum: an antiparasitic drug target. J Biol Chem, 287, 1426-1434. PubMed id: 22117061
Date:
07-Nov-11     Release date:   30-Nov-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8IDQ9  (Q8IDQ9_PLAF7) -  Phosphoethanolamine N-methyltransferase from Plasmodium falciparum (isolate 3D7)
Seq:
Struc:
266 a.a.
259 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.2.1.1.103  - phosphoethanolamine N-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: phosphoethanolamine + S-adenosyl-L-methionine = N-methylethanolamine phosphate + S-adenosyl-L-homocysteine + H+
phosphoethanolamine
+ S-adenosyl-L-methionine
= N-methylethanolamine phosphate
+
S-adenosyl-L-homocysteine
Bound ligand (Het Group name = PC)
matches with 81.82% similarity
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Biol Chem 287:1426-1434 (2012)
PubMed id: 22117061  
 
 
Structure and reaction mechanism of phosphoethanolamine methyltransferase from the malaria parasite Plasmodium falciparum: an antiparasitic drug target.
S.G.Lee, Y.Kim, T.D.Alpert, A.Nagata, J.M.Jez.
 
  ABSTRACT  
 
No abstract given.

 

 

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