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PDBsum entry 3nd6

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3nd6
Jmol
Contents
Protein chains
(+ 0 more) 152 a.a.
Ligands
ATP ×6
Waters ×413
PDB id:
3nd6
Name: Transferase
Title: Crystal structure of phosphopantetheine adenylyltransferase complex with atp from enterococcus faecalis
Structure: Phosphopantetheine adenylyltransferase. Chain: a, b, c, d, e, f. Synonym: ppat, pantetheine-phosphate adenylyltransferase, d coa pyrophosphorylase. Engineered: yes
Source: Enterococcus faecalis. Streptococcus faecalis. Organism_taxid: 1351. Gene: coad. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.30Å     R-factor:   0.206     R-free:   0.245
Authors: H.J.Yoon,H.H.Lee,S.W.Suh
Key ref: H.J.Yoon et al. (2011). Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine. Mol Cells, 32, 431-435. PubMed id: 21912874
Date:
07-Jun-10     Release date:   22-Jun-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q831P9  (COAD_ENTFA) -  Phosphopantetheine adenylyltransferase
Seq:
Struc:
163 a.a.
152 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.7.3  - Pantetheine-phosphate adenylyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Coenzyme A Biosynthesis (late stages)
      Reaction: ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
ATP
Bound ligand (Het Group name = ATP)
corresponds exactly
+ pantetheine 4'-phosphate
= diphosphate
+ 3'-dephospho-CoA
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     biosynthetic process   2 terms 
  Biochemical function     catalytic activity     6 terms  

 

 
    reference    
 
 
Mol Cells 32:431-435 (2011)
PubMed id: 21912874  
 
 
Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine.
H.J.Yoon, J.Y.Kang, B.Mikami, H.H.Lee, S.W.Suh.
 
  ABSTRACT  
 
No abstract given.