5FRD

Name : Structure of a thermophilic esterase

Revelation date : 25-May-2016

Family : 6_AlphaBeta_hydrolase

Gene_locus : arcfu-est2

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

Comment
Sayer, C., Finnigan, W., Isupov, M.N., Levisson, M., Kengen, S.W.M., van der Oost, J., Harmer, N., Littlechild, J.A.:
A thermophilic esterase with high activity towards short- to medium-chain
p-nitrophenyl carboxylic esters with optimal activity towards the valerate ester.
The AF-Est2 has good solvent and pH stability and is very thermostable,
showing no loss of activity after incubation for 30min at 80 C.
The structure reveals a bound CoA molecule in the vicinity of the active site

Ligand : substrate Coenzyme-A Ligand in structure: Ligplot

References (1)

Title : Structural and biochemical characterisation of Archaeoglobus fulgidus esterase reveals a bound CoA molecule in the vicinity of the active site - Sayer_2016_Sci.Rep_6_25542
Author(s) : Sayer C , Finnigan W , Isupov MN , Levisson M , Kengen SW , Van der Oost J , Harmer NJ , Littlechild JA
Ref : Sci Rep , 6 :25542 , 2016
Abstract :
PubMedSearch : Sayer_2016_Sci.Rep_6_25542
PubMedID: 27160974
Gene_locus related to this paper: arcfu-est2

Representative scheme of Prolylcarboxypeptidase structure and an image from PDBsum server

Databases

PDB-Sum : 5FRD Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server

FSSP : 5FRD Fold classification based on Structure-Structure alignment of Proteins - FSSP server

SCOP : 5FRD Structural Classification Of Protein - SCOP server

PROTEOPEDIA : 5FRD 3D, interactive encyclopedia of proteins - PROTEOPEDIA server