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PDBsum entry 2vor
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protein ligands metals links
Ligase PDB id
2vor

 

 

 

 

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Contents
Protein chain
442 a.a. *
Ligands
ACP
GOL ×2
Metals
_CO ×4
Waters ×122
* Residue conservation analysis
PDB id:
2vor
Name: Ligase
Title: Crystal structures of mycobacterium tuberculosis folylpolyglutamate synthase complexed with adp and amppcp
Structure: Folylpolyglutamate synthase protein folc. Chain: a. Synonym: folylpolyglutamate synthase, folylpoly-gamma-glutamate synthetase, fpgs, folylpolyglutamate synthase. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.30Å     R-factor:   0.178     R-free:   0.223
Authors: P.G.Young,E.N.Baker,P.Metcalf,C.A.Smith
Key ref: P.G.Young et al. (2008). Structures of mycobacterium tuberculosisfolylpolyglut synthase complexed with ADP and amppcp.. Acta crystallogr ,Sect d, 64, 745. PubMed id: 18566510
Date:
19-Feb-08     Release date:   01-Jul-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O53174  (O53174_MYCTO) -  tetrahydrofolate synthase from Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Seq:
Struc: 		487 a.a.
442 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.3.2.17  - tetrahydrofolate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Folate Biosynthesis (late stages)
      Reaction: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + L-glutamate + ATP = (6S)- 5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + phosphate + H+
(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n)
 + L-glutamate
 + ATP
 = (6S)- 5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1)
 +
ADP
Bound ligand (Het Group name = ACP)
matches with 81.25% similarity 		+ phosphate
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20350571 P.Wang, Q.Wang, Y.Yang, J.K.Coward, A.Nzila, P.F.Sims, and J.E.Hyde (2010).
Characterisation of the bifunctional dihydrofolate synthase-folylpolyglutamate synthase from Plasmodium falciparum; a potential novel target for antimalarial antifolate inhibition.
  Mol Biochem Parasitol, 172, 41-51.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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