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Ligase PDB id
2d7u
Jmol
Contents
Protein chain
321 a.a. *
Waters ×106
* Residue conservation analysis
PDB id:
2d7u
Name: Ligase
Title: Crystal structure of hypothetical adenylosuccinate synthetas from pyrococcus horikoshii ot3
Structure: Adenylosuccinate synthetase. Chain: a. Synonym: imp--aspartate ligase, adss, ampsase. Engineered: yes
Source: Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PQS)
Resolution:
2.50Å     R-factor:   0.236     R-free:   0.285
Authors: Y.Xie,S.Kishisita,K.Murayama,M.Shirouzu,S.Yokoyama,Riken Str Genomics/proteomics Initiative (Rsgi)
Key ref: Y.Xie et al. Crystal structure of hypothetical adenylosuccinate synthetase, Ph0438 from pyrococcus horikoshii ot3. To be published,
Date:
29-Nov-05     Release date:   29-May-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O58187  (PURA_PYRHO) -  Adenylosuccinate synthetase
Seq:
Struc:
339 a.a.
321 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.6.3.4.4  - Adenylosuccinate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
AMP and GMP Biosynthesis
      Reaction: GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)- AMP
GTP
+ IMP
+ L-aspartate
= GDP
+ phosphate
+ N(6)-(1,2-dicarboxyethyl)- AMP
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     purine nucleotide biosynthetic process   1 term 
  Biochemical function     nucleotide binding     6 terms