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PDBsum entry 4f5l

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protein ligands Protein-protein interface(s) links
Transferase PDB id
4f5l
Jmol
Contents
Protein chains
399 a.a.
Ligands
EDO ×13
Waters ×1237
PDB id:
4f5l
Name: Transferase
Title: A theoretical optimized mutant for the conversion of substra specificity and activity of aspartate aminotransferase to t aminotransferase: chimera p7.
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: 469008.
Resolution:
1.40Å     R-factor:   0.162     R-free:   0.181
Authors: T.A.Addington,A.J.Fisher,M.D.Toney
Key ref: T.A.Addington et al. Janus: an algorithm for ranking functional importance residues from protein sequence alignments.. To be published, .
Date:
13-May-12     Release date:   15-May-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00509  (AAT_ECOLI) -  Aspartate aminotransferase
Seq:
Struc:
396 a.a.
399 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 20 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 = EDO)
matches with 44.44% 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