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PDBsum entry 3uc5

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protein ligands links
Transferase PDB id
3uc5

 

 

 

 

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Contents
Protein chain
157 a.a.
Ligands
ATP
Waters ×59
PDB id:
3uc5
Name: Transferase
Title: Phosphopantetheine adenylyltransferase from mycobacterium tuberculosis complexed with atp
Structure: Phosphopantetheine adenylyltransferase. Chain: a. Synonym: dephospho-coa pyrophosphorylase, pantetheine-phosphate adenylyltransferase, ppat. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: coad, kdtb, rv2965c, mt3043, mtcy349.22, u0002e. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.70Å     R-factor:   0.179     R-free:   0.222
Authors: V.I.Timofeev,E.A.Smirnova,L.A.Chupova,R.S.Esipov,I.P.Kuranova
Key ref: V.Timofeev et al. (2012). X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction. Acta Crystallogr D Biol Crystallogr, 68, 1660-1670. PubMed id: 23151631
Date:
26-Oct-11     Release date:   07-Nov-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P9WPA5  (COAD_MYCTU) -  Phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Seq:
Struc:
161 a.a.
157 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: (R)-4'-phosphopantetheine + ATP + H+ = 3'-dephospho-CoA + diphosphate
(R)-4'-phosphopantetheine
+
ATP
Bound ligand (Het Group name = ATP)
corresponds exactly
+ H(+)
= 3'-dephospho-CoA
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Acta Crystallogr D Biol Crystallogr 68:1660-1670 (2012)
PubMed id: 23151631  
 
 
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction.
V.Timofeev, E.Smirnova, L.Chupova, R.Esipov, I.Kuranova.
 
  ABSTRACT  
 
No abstract given.

 

 

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