1AUR

PMSF-INHIBITED CARBOXYLESTERASE FROM PSEUDOMONAS FLUORESCENS


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.254 
  • R-Value Work: 0.181 
  • R-Value Observed: 0.181 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity.

Kim, K.K.Song, H.K.Shin, D.H.Hwang, K.Y.Choe, S.Yoo, O.J.Suh, S.W.

(1997) Structure 5: 1571-1584

  • DOI: https://doi.org/10.1016/s0969-2126(97)00306-7
  • Primary Citation of Related Structures:  
    1AUO, 1AUR

  • PubMed Abstract: 

    A group of esterases, classified as carboxylesterases, hydrolyze carboxylic ester bonds with relatively broad substrate specificity and are useful for stereospecific synthesis and hydrolysis of esters. One such carboxylesterase from Pseudomonas fluorescens is a homodimeric enzyme, consisting of 218-residue subunits. It shows a limited sequence similarity to some members of the alpha/beta hydrolase superfamily. Although crystal structures of a number of serine esterases and lipases have been reported, structural information on carboxylesterases is very limited. This study was undertaken in order to provide such information and to understand a structural basis for the substrate specificity of this carboxylesterase.


  • Organizational Affiliation

    Department of Chemistry, College of Natural Sciences, Seoul National University, Korea.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CARBOXYLESTERASE
A, B
218Pseudomonas fluorescensMutation(s): 0 
EC: 3.1.1.1
UniProt
Find proteins for Q53547 (Pseudomonas fluorescens)
Explore Q53547 
Go to UniProtKB:  Q53547
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ53547
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.254 
  • R-Value Work: 0.181 
  • R-Value Observed: 0.181 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.49α = 90
b = 81.49β = 90
c = 144.53γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
PROCORdata reduction
FSSCALEdata scaling
X-PLORphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-03-04
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-04-18
    Changes: Data collection, Other