2ZE0

Alpha-glucosidase GSJ


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.205 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of GH13 alpha-glucosidase GSJ from one of the deepest sea bacteria

Shirai, T.Hung, V.S.Morinaka, K.Kobayashi, T.Ito, S.

(2008) Proteins 73: 126-133

  • DOI: https://doi.org/10.1002/prot.22044
  • Primary Citation of Related Structures:  
    2ZE0

  • PubMed Abstract: 

    The crystal structure of the GH13 alpha-glucosidase (GSJ) from deep-sea bacterium Geobacillus sp. strain HTA-462 was determined to a 2.0 A resolution. Comparisons of the GSJ structure with that of other GH13 enzymes with different catalytic activities revealed that the catalytic cleft of GSJ was widely opened when compared with the homologues. The wide opening of the catalytic cleft originated from conformational changes of active site residues and disorder of the regions close to the catalytic center. This structural feature of GSJ would explain the ability of this enzyme to accept a wide variety of nonsugar molecules as acceptors in the transglycosylation reaction.


  • Organizational Affiliation

    Department of Bioscience, Nagahama Institute of Bioscience and Technology, 1266 Tamura, Nagahama 526-0829, Japan. t_shirai@nagahama-i-bio.ac.jp


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Alpha-glucosidase555Geobacillus sp. HTA-462Mutation(s): 0 
Gene Names: gsj
EC: 3.2.1.20
UniProt
Find proteins for Q33E90 (Geobacillus sp. HTA-462)
Explore Q33E90 
Go to UniProtKB:  Q33E90
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ33E90
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CA
Query on CA

Download Ideal Coordinates CCD File 
B [auth A]CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.205 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 103.829α = 90
b = 90.621β = 109.4
c = 72.285γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data collection
HKL-2000data reduction
SCALEPACKdata scaling
AMoREphasing
CNSrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-12-18
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.2: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description