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PDBsum entry 3pph

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protein Protein-protein interface(s) links
Transferase PDB id
3pph

 

 

 

 

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Contents
Protein chains
756 a.a.
Waters ×51
PDB id:
3pph
Name: Transferase
Title: Crystal structure of the candida albicans methionine synthase by surface entropy reduction, threonine variant
Structure: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase. Chain: a, b. Synonym: cobalamin-independent methionine synthase, methionine synthase, vitamin-b12 independent isozyme. Engineered: yes. Mutation: yes
Source: Candida albicans. Yeast. Organism_taxid: 5476. Strain: bwp17. Gene: cao19.10083, cao19.2551, met6. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.80Å     R-factor:   0.213     R-free:   0.276
Authors: D.Ubhi,K.Kavanagh,A.F.Monzingo,J.D.Robertus
Key ref: D.Ubhi et al. (2011). Structure of Candida albicans methionine synthase determined by employing surface residue mutagenesis. Arch Biochem Biophys, 513, 19-26. PubMed id: 21689631
Date:
24-Nov-10     Release date:   12-Oct-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P82610  (METE_CANAL) -  5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase from Candida albicans (strain SC5314 / ATCC MYA-2876)
Seq:
Struc:
 
Seq:
Struc:
767 a.a.
756 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.1.1.14  - 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine
5-methyltetrahydropteroyltri-L-glutamate
+ L-homocysteine
= tetrahydropteroyltri-L-glutamate
+ L-methionine
      Cofactor: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Arch Biochem Biophys 513:19-26 (2011)
PubMed id: 21689631  
 
 
Structure of Candida albicans methionine synthase determined by employing surface residue mutagenesis.
D.Ubhi, K.L.Kavanagh, A.F.Monzingo, J.D.Robertus.
 
  ABSTRACT  
 
No abstract given.

 

 

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