_EC Asparagine synthase (glutamine-hydrolyzing). 1 PDB entries  
EC 6.-.-.- Ligases. [1,685 PDB entries]
EC 6.3.-.- Forming carbon-nitrogen bonds. [864 PDB entries]
EC 6.3.5.- Carbon--nitrogen ligases with glutamine as amido-N-donor. [84 PDB entries]
EC Asparagine synthase (glutamine-hydrolyzing). [1 PDB entries]    

Reaction: Atp + L-aspartate + L-glutamine + H(2)O = amp + diphosphate + L-asparagine + L-glutamate.

+ H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): AS-B. Asparagine synthetase (glutamine-hydrolyzing). Asparagine synthetase B. Glutamine-dependent asparagine synthetase.
Comments: The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel. The enzyme catalyzes three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. The C-terminal active site mediates both the synthesis of a beta- aspartyl-AMP intermediate and its subsequent reaction with ammonia. The ammonia released is channeled to the other active site to yield asparagine.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 1 PDB entries in enzyme class E.C.

  PDB code Protein
Crystal structure of asparagine synthetase b from escherichia coli
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (497 residues) CATH domains:
Bound ligands:   Het Group GLN corresponds to enzyme reactant L-glutamine
  Het Group AMP corresponds to enzyme product AMP