spacer
spacer

PDBsum entry 4m0g

Go to PDB code: 
protein metals Protein-protein interface(s) links
Ligase PDB id
4m0g
Jmol
Contents
Protein chains
421 a.a.
Metals
_CL
Waters ×273
PDB id:
4m0g
Name: Ligase
Title: The crystal structure of an adenylosuccinate synthetase from anthracis str. Ames ancestor.
Structure: Adenylosuccinate synthetase. Chain: a, b. Synonym: ampsase, adss, imp--aspartate ligase. Engineered: yes. Mutation: yes
Source: Bacillus anthracis. Anthrax,anthrax bacterium. Organism_taxid: 261594. Strain: ames ancestor. Gene: bas5320, ba_5716, gbaa_5716, pura. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.15Å     R-factor:   0.194     R-free:   0.243
Authors: K.Tan,M.Zhou,R.Zhang,K.Kwon,W.F.Anderson,A.Joachimiak,Midwes For Structural Genomics (Mcsg)
Key ref: K.Tan et al. The crystal structure of an adenylosuccinate syntheta bacillus anthracis str. Ames ancestor.. To be published, .
Date:
01-Aug-13     Release date:   14-Aug-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q81JI9  (PURA_BACAN) -  Adenylosuccinate synthetase
Seq:
Struc:
429 a.a.
421 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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     'de novo' AMP biosynthetic process   2 terms 
  Biochemical function     nucleotide binding     6 terms