8Z43

Beta-galactosidase from Bacteroides xylanisolvens (E350G, ligand-free)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.91 Å
  • R-Value Free: 0.202 
  • R-Value Work: 0.174 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.0 of the entry. See complete history


Literature

A beta-Galactosidase acting on unique galactosides: the structure and function of a beta-1,2-galactosidase from Bacteroides xylanisolvens, an intestinal bacterium

Nakazawa, Y.Kageyama, M.Matsuzawa, T.Liang, Z.Kobayashi, K.Shimizu, H.Masuhiro, M.Motouchi, S.Kumano, S.Tanaka, N.Kuramochi, K.Nakai, H.Taguchi, H.Nakajima, M.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-galactosidase
A, B
551Bacteroides xylanisolvens XB1AMutation(s): 1 
Gene Names: BXY_22780
UniProt
Find proteins for D6CYU7 (Bacteroides xylanisolvens XB1A)
Explore D6CYU7 
Go to UniProtKB:  D6CYU7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupD6CYU7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.91 Å
  • R-Value Free: 0.202 
  • R-Value Work: 0.174 
  • Space Group: I 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 144.699α = 90
b = 51.062β = 90.415
c = 180.085γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling
MOLREPphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Not funded--

Revision History  (Full details and data files)

  • Version 1.0: 2025-01-01
    Type: Initial release