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protein Protein-protein interface(s) links
Ligase PDB id
1vl2
Jmol
Contents
Protein chains
398 a.a. *
Waters ×1184
* Residue conservation analysis
PDB id:
1vl2
Name: Ligase
Title: Crystal structure of argininosuccinate synthase (tm1780) fro thermotoga maritima at 1.65 a resolution
Structure: Argininosuccinate synthase. Chain: a, b, c, d. Synonym: citrulline--aspartate ligase. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: argg, tm1780. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
1.65Å     R-factor:   0.179     R-free:   0.209
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref: Joint center for structural genomics (jcsg) Crystal structure of argininosuccinate synthase (tm1780) from thermotoga maritima at 1.65 a resolution. To be published,
Date:
08-Jul-04     Release date:   17-Aug-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9X2A1  (ASSY_THEMA) -  Argininosuccinate synthase
Seq:
Struc:
409 a.a.
398 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.3.4.5  - Argininosuccinate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Urea Cycle and Arginine Biosynthesis
      Reaction: ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)- (L-arginino)succinate
ATP
+ L-citrulline
+ L-aspartate
= AMP
+ diphosphate
+ N(omega)- (L-arginino)succinate
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     cellular amino acid biosynthetic process   2 terms 
  Biochemical function     nucleotide binding     4 terms