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PDBsum entry 3f6t

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3f6t
Jmol
Contents
Protein chains
515 a.a. *
Ligands
EDO ×5
Waters ×571
* Residue conservation analysis
PDB id:
3f6t
Name: Transferase
Title: Crystal structure of aspartate aminotransferase (E.C. 2.6.1. (Yp_194538.1) from lactobacillus acidophilus ncfm at 2.15 a resolution
Structure: Aspartate aminotransferase. Chain: a, b. Engineered: yes
Source: Lactobacillus acidophilus ncfm. Organism_taxid: 272621. Gene: lba1695, yp_194538.1. Expressed in: escherichia coli.
Resolution:
2.15Å     R-factor:   0.180     R-free:   0.238
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref: Joint center for structural genomics (jcsg) Crystal structure of aspartate aminotransferase (e.C. 2.6.1.1) (yp_194538.1) from lactobacillus acidophilus ncfm at 2.15 a resolution. To be published, .
Date:
06-Nov-08     Release date:   09-Dec-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q5FIG7  (Q5FIG7_LACAC) -  Aspartate aminotransferase
Seq:
Struc:
 
Seq:
Struc:
532 a.a.
515 a.a.*
Key:    PfamA domain  PfamB 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
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!
  Biological process     biosynthetic process   1 term 
  Biochemical function     catalytic activity     6 terms