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PDBsum entry 2vor

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protein ligands metals links
Ligase PDB id
2vor
Jmol
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-gluta 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
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O53174  (O53174_MYCTU) -  Folylpolyglutamate synthase
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: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1)
ATP
+ tetrahydropteroyl-(gamma-Glu)(n)
+ L-glutamate
=
ADP
Bound ligand (Het Group name = ACP)
matches with 81.25% similarity
+ phosphate
+ tetrahydropteroyl-(gamma-Glu)(n+1)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     growth   4 terms 
  Biochemical function     nucleotide binding     8 terms  

 

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.  
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