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PDBsum entry 3syt

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protein ligands Protein-protein interface(s) links
Ligase PDB id
3syt

 

 

 

 

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Contents
Protein chains
660 a.a.
Ligands
GLU ×4
NAD ×4
AMP ×4
POP ×4
GOL ×2
Waters ×486
PDB id:
3syt
Name: Ligase
Title: Crystal structure of glutamine-dependent NAD+ synthetase from m. Tuberculosis bound to amp/ppi, NAD+, and glutamate
Structure: Glutamine-dependent NAD(+) synthetase. Chain: a, b, c, d. Synonym: NAD(+) synthase [glutamine-hydrolyzing]. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: mt2513, mtcy428.08, nade, rv2438c. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.65Å     R-factor:   0.157     R-free:   0.200
Authors: W.Chuenchor,B.Gerratana
Key ref: W.Chuenchor et al. (2012). Regulation of the intersubunit ammonia tunnel in Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase. Biochem J, 443, 417-426. PubMed id: 22280445
Date:
18-Jul-11     Release date:   11-Apr-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P9WJJ3  (NADE_MYCTU) -  Glutamine-dependent NAD(+) synthetase from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Seq:
Struc:
 
Seq:
Struc:
679 a.a.
660 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.3.5.1  - NAD(+) synthase (glutamine-hydrolyzing).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: deamido-NAD+ + L-glutamine + ATP + H2O = L-glutamate + AMP + diphosphate + NAD+ + H+
deamido-NAD(+)
+ L-glutamine
+ ATP
+ H2O
= L-glutamate
+
AMP
Bound ligand (Het Group name = POP)
corresponds exactly
+ diphosphate
+
NAD(+)
Bound ligand (Het Group name = GLU)
corresponds exactly
+ H(+)
Bound ligand (Het Group name = NAD)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Biochem J 443:417-426 (2012)
PubMed id: 22280445  
 
 
Regulation of the intersubunit ammonia tunnel in Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase.
W.Chuenchor, T.I.Doukov, M.Resto, A.Chang, B.Gerratana.
 
  ABSTRACT  
 
No abstract given.

 

 

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