Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
5GP Guanosine-5'-monophosphate
ADP Adenosine-5'-diphosphate
MG Magnesium ion
SF4 Iron/sulfur cluster
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1AO0   PDBj   RCSB PDB   PDBe
Header : GLUTAMINE AMIDOTRANSFERASE
Title : GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE FROM B. SUBTILIS COMPLEXED WITH ADP AND GMP
Release Data : 1997-11-12
Compound :
mol_id molecule chains
1 GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE AMIDOTRANSFERASE A,B,C,D
ec: 2.4.2.14
Source :
mol_id organism_scientific expression_system
1 Bacillus subtilis  (taxid:1423) Escherichia coli  (taxid:562)
gene: PURF
expression_system_strain: TX158
expression_system_plasmid: PGZ1 (PURF+ FRAGMENT INSERTED INTO PUC18)
Authors : Tomchick, D.R., Smith, J.L.
Keywords : TRANSFERASE, GLUTAMINE AMIDOTRANSFERASE, PRTASE, PURINE BIOSYNTHESIS, PHOSPHORIBOSYLTRANSFERASE, GLYCOSYLTRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.8 Å )
Citation :

Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides.

Chen, S.,Tomchick, D.R.,Wolle, D.  et al.
(1997)  Biochemistry  36 : 10718 - 10726

PubMed: 9271502
DOI: 10.1021/bi9711893

Chain : A, B, C, D
UniProt : P00497 (PUR1_BACSU)
Reaction: EC: Evidence:
Physiological Direction:
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5- phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine 2.4.2.14 HAMAP- Rule:MF_01931, PubMed:6794613
-