1AMN

Name : Torpedo acetylcholinesterase complexed with transition state analog with m-(N,N,N-trimethyammonio)trifluoroacetophenone (TMTFA, NAF)

Revelation date : 03-Apr-1996

Family : ACHE

Gene_locus : torca-ACHE

PDB file : ESTHER: header of PDB entry RCSB: Full entry

Comment
TMTFA is an equilibrium mixture of the free ketone and ketone hydrate NAF in aqueous solution, with a hydration equilibrium constant of 60 000

Ligand : 02

References (2)

Title : A preliminary comparison of structural models for catalytic intermediates of acetylcholinesterase - Silman_1999_Chem.Biol.Interact_119-120_43

Author(s) : Silman I , Millard CB , Ordentlich A , Greenblatt HM , Harel M , Barak D , Shafferman A , Sussman JL

Ref : Chemico-Biological Interactions , 119-120 :43 , 1999

Abstract : Silman_1999_Chem.Biol.Interact_119-120_43

ESTHER : Silman_1999_Chem.Biol.Interact_119-120_43

PubMedSearch : Silman_1999_Chem.Biol.Interact_119-120_43

PubMedID: 10421437

Gene_locus related to this paper: torca-ACHE

Title : The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase. -

Author(s) : Harel M , Quinn DM , Nair HK , Silman I , Sussman JL

Ref : Journal of the American Chemical Society , 118 :2340 , 1996

PubMedID:

Gene_locus related to this paper: torca-ACHE

1AMN

References (2)

Representative scheme of Prolylcarboxypeptidase structure and an image from PDBsum server

Databases

1AMN

References (2)

1. A preliminary comparison of structural models for catalytic intermediates of acetylcholinesterase

2. The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase.

Representative scheme of Prolylcarboxypeptidase structure and an image from PDBsum server

Databases