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PDBsum entry 1asc

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protein ligands links
Aminotransferase PDB id
1asc
Jmol
Contents
Protein chain
396 a.a. *
Ligands
NPL
Waters ×22
* Residue conservation analysis
PDB id:
1asc
Name: Aminotransferase
Title: The structural basis for the reduced activity of the d223a(d active site mutant of e. Coli aspartate aminotransferase
Structure: Aspartate aminotransferase. Chain: a. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
2.40Å     R-factor:   0.214    
Authors: C.Schumacher,D.Ringe
Key ref: C.Schumacher and d.ringe The structural basis for the reduced activity of the d223a(d222a) active site mutant of e. Coli aspartate aminotransferase. To be published, .
Date:
27-Aug-93     Release date:   30-Apr-94    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00509  (AAT_ECOLI) -  Aspartate aminotransferase
Seq:
Struc:
396 a.a.
396 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.2.6.1.1  - Aspartate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
L-aspartate
+ 2-oxoglutarate
= oxaloacetate
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = NPL) matches with 83.33% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     biosynthetic process   4 terms 
  Biochemical function     catalytic activity     8 terms