spacer
spacer

PDBsum entry 2d65

Go to PDB code: 
protein ligands links
Transferase PDB id
2d65
Jmol
Contents
Protein chain
396 a.a. *
Ligands
SO4
PLP
Waters ×237
* Residue conservation analysis
PDB id:
2d65
Name: Transferase
Title: Aspartate aminotransferase mutant mabc
Structure: Aspartate aminotransferase. Chain: a. Synonym: transaminase a, aspat. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
Resolution:
2.30Å     R-factor:   0.166     R-free:   0.202
Authors: Y.Tanaka,N.Nakagawa,H.Tada,T.Yano,R.Masui,S.Kuramitsu
Key ref: Y.Tanaka et al. The structures of aspartate aminotransferase with mutations of non-Active-Site residues. To be published, .
Date:
09-Nov-05     Release date:   14-Nov-06    
PROCHECK
Go to PROCHECK summary
 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 14 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
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) matches with 93.75% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     biosynthetic process   2 terms 
  Biochemical function     catalytic activity     6 terms