1BXS

SHEEP LIVER CLASS 1 ALDEHYDE DEHYDROGENASE WITH NAD BOUND


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.235 
  • R-Value Observed: 0.235 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases.

Moore, S.A.Baker, H.M.Blythe, T.J.Kitson, K.E.Kitson, T.M.Baker, E.N.

(1998) Structure 6: 1541-1551

  • DOI: https://doi.org/10.1016/s0969-2126(98)00152-x
  • Primary Citation of Related Structures:  
    1BXS

  • PubMed Abstract: 

    . Enzymes of the aldehyde dehydrogenase family are required for the clearance of potentially toxic aldehydes, and are essential for the production of key metabolic regulators. The cytosolic, or class 1, aldehyde dehydrogenase (ALDH1) of higher vertebrates has an enhanced specificity for all-trans retinal, oxidising it to the powerful differentiation factor all-trans retinoic acid. Thus, ALDH1 is very likely to have a key role in vertebrate development.


  • Organizational Affiliation

    Institute of Molecular Biosciences, Massey University, Private Bag, 11-222, Palmerston North, New Zealand.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ALDEHYDE DEHYDROGENASE
A, B, C, D
501Ovis ariesMutation(s): 0 
EC: 1.2.1.3
UniProt
Find proteins for P51977 (Ovis aries)
Explore P51977 
Go to UniProtKB:  P51977
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP51977
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.35 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.235 
  • R-Value Observed: 0.235 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 80.689α = 110.47
b = 87.625β = 105.63
c = 90.84γ = 103.56
Software Package:
Software NamePurpose
AMoREphasing
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-04-27
    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: 2023-08-09
    Changes: Database references, Derived calculations, Refinement description