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protein Protein-protein interface(s) links
Ligase PDB id
2yya
Jmol
Contents
Protein chains
423 a.a. *
Waters ×89
* Residue conservation analysis
PDB id:
2yya
Name: Ligase
Title: Crystal structure of gar synthetase from aquifex aeolicus
Structure: Phosphoribosylamine--glycine ligase. Chain: a, b. Synonym: gars, glycinamide ribonucleotide synthetase, phosphoribosylglycinamide synthetase. Engineered: yes
Source: Aquifex aeolicus. Organism_taxid: 63363. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.40Å     R-factor:   0.225     R-free:   0.249
Authors: S.Baba,M.Kanagawa,S.Kuramitsu,S.Yokoyama,G.Kawai,G.Sampei,Ri Structural Genomics/proteomics Initiative (Rsgi)
Key ref: G.Sampei et al. (2010). Crystal structures of glycinamide ribonucleotide synthetase, PurD, from thermophilic eubacteria. J Biochem, 148, 429-438. PubMed id: 20716513 Ref: Full text
Date:
27-Apr-07     Release date:   30-Oct-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O66949  (PUR2_AQUAE) -  Phosphoribosylamine--glycine ligase
Seq:
Struc:
424 a.a.
423 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.3.4.13  - Phosphoribosylamine--glycine ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Purine Biosynthesis (early stages)
      Reaction: ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1- (5-phospho-D-ribosyl)glycinamide
ATP
+ 5-phospho-D-ribosylamine
+ glycine
= ADP
+ phosphate
+ N(1)- (5-phospho-D-ribosyl)glycinamide
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     purine base biosynthetic process   2 terms 
  Biochemical function     catalytic activity     6 terms  

 

 
    reference    
 
 
Full text J Biochem 148:429-438 (2010)
PubMed id: 20716513  
 
 
Crystal structures of glycinamide ribonucleotide synthetase, PurD, from thermophilic eubacteria.
G.Sampei, S.Baba, M.Kanagawa, H.Yanai, T.Ishii, H.Kawai, Y.Fukai, A.Ebihara, N.Nakagawa, G.Kawai.
 
  ABSTRACT  
 
No abstract given.