PDBsum entry 1oxo

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protein ligands Protein-protein interface(s) links
Aminotransferase PDB id
Jmol PyMol
Protein chains
401 a.a. *
IK2 ×2
Waters ×541
* Residue conservation analysis
PDB id:
Name: Aminotransferase
Title: Aspartate aminotransferase, h-asp complex, open conformation
Structure: Aspartate aminotransferase. Chain: a, b. Engineered: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Organelle: mitochondria. Expressed in: unidentified. Expression_system_taxid: 32644
Biol. unit: Dimer (from PQS)
2.30Å     R-factor:   0.128    
Authors: E.Hohenester,T.Schirmer,J.N.Jansonius
Key ref: Z.Marković-Housley et al. (1996). Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase. Eur J Biochem, 236, 1025-1032. PubMed id: 8665890
23-Dec-95     Release date:   10-Jun-96    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P00508  (AATM_CHICK) -  Aspartate aminotransferase, mitochondrial
423 a.a.
401 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 1: E.C.  - Aspartate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
+ 2-oxoglutarate
= oxaloacetate
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = IK2) matches with 68.00% similarity
   Enzyme class 2: E.C.  - Kynurenine--oxoglutarate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
+ 2-oxoglutarate
= 4-(2-aminophenyl)-2,4-dioxobutanoate
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mitochondrion   2 terms 
  Biological process     L-kynurenine metabolic process   8 terms 
  Biochemical function     transferase activity     7 terms  


Eur J Biochem 236:1025-1032 (1996)
PubMed id: 8665890  
Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase.
Z.Marković-Housley, T.Schirmer, E.Hohenester, A.R.Khomutov, R.M.Khomutov, M.Y.Karpeisky, E.Sandmeier, P.Christen, J.N.Jansonius.
The interaction of mitochondrial aspartate aminotransferase with hydroxylamine and five derivatives (in which the hydroxyl hydrogen is replaced by the side chain of naturally occurring amino acids) was investigated by X-ray diffraction as well as by kinetic and spectral measurements with the enzyme in solution. The inhibitors react with pyridoxal 5'-phosphate in the enzyme active site, both in solution and in the crystalline state, in a reversible single-step reaction forming spectrally distinct oxime adducts. Dissociation constants determined in solution range from 10(-8) M to 10(-6) M depending on the nature of the side-chain group. The crystal structures of the adducts of mitochondrial aspartate aminotransferase with the monocarboxylic analogue of L-aspartate in the open and closed enzyme conformation were determined at 0.23-nm and 0.25-nm resolution, respectively. This inhibitor binds to both the open and closed crystal forms of the enzyme without disturbing the crystalline order. Small differences in the conformation of the cofactor pyridoxal phosphate were detected between the omega-carboxylate of the inhibitor and Arg292 of the neighbouring subunit is mainly responsible for the attainment of near-coplanarity of the aldimine bond with the pyridine ring in the oxime adducts. Studies with a fluorescent probe aimed to detect shifts in the open/closed conformational equilibrium of the enzyme in oxime complexes showed that the hydroxylamine-derived inhibitors, even those containing a carboxylate group, do not induce the 'domain closure' in solution. This is probably due to the absence of the alpha-carboxylate group in the monocarboxylic hydroxylamine-derived inhibitors, emphasizing that both carboxylates of the substrates L-Asp and L-Glu are essential for stabilizing the closed form of aspartate aminotransferase.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19997759 M.A.Khomutov, S.Mandal, J.Weisell, N.Saxena, A.R.Simonian, J.Vepsalainen, R.Madhubala, and S.N.Kochetkov (2010).
Novel convenient synthesis of biologically active esters of hydroxylamine.
  Amino Acids, 38, 509-517.  
16354669 A.Järvinen, T.A.Keinänen, N.A.Grigorenko, A.R.Khomutov, A.Uimari, J.Vepsäläinen, A.Närvänen, L.Alhonen, and J.Jänne (2006).
Guide molecule-driven stereospecific degradation of alpha-methylpolyamines by polyamine oxidase.
  J Biol Chem, 281, 4589-4595.  
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