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PDBsum entry 4f5i

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protein ligands Protein-protein interface(s) links
Transferase PDB id
4f5i
Jmol
Contents
Protein chains
400 a.a.
Ligands
MPD
Waters ×743
PDB id:
4f5i
Name: Transferase
Title: Substrate specificity conversion of e. Coli pyridoxal-5'-pho dependent aspartate aminotransferase to tyrosine aminotrans chimera p4.
Structure: Aspartate aminotransferase. Chain: a, b. Synonym: aspat, transaminase a. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: aat, aspc, b0928, jw0911. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.175     R-free:   0.212
Authors: T.A.Addington,A.J.Fisher,M.D.Toney
Key ref: T.A.Addington et al. (2013). Janus: prediction and ranking of mutations required for functional interconversion of enzymes. J Mol Biol, 425, 1378-1389. PubMed id: 23396064 DOI: 10.1016/j.jmb.2013.01.034
Date:
13-May-12     Release date:   13-Feb-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00509  (AAT_ECOLI) -  Aspartate aminotransferase
Seq:
Struc:
396 a.a.
400 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 18 residue positions (black crosses)

 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
Bound ligand (Het Group name = MPD)
matches with 54.55% similarity
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
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  

 

 
    reference    
 
 
DOI no: 10.1016/j.jmb.2013.01.034 J Mol Biol 425:1378-1389 (2013)
PubMed id: 23396064  
 
 
Janus: prediction and ranking of mutations required for functional interconversion of enzymes.
T.A.Addington, R.W.Mertz, J.B.Siegel, J.M.Thompson, A.J.Fisher, V.Filkov, N.M.Fleischman, A.A.Suen, C.Zhang, M.D.Toney.
 
  ABSTRACT  
 
No abstract given.