2DLD

D-LACTATE DEHYDROGENASE COMPLEXED WITH NADH AND OXAMATE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.297 
  • R-Value Observed: 0.195 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Dehydrogenases Engineering to Correct Substrate Inhibition in a Commercial Dehydrogenase

Bernard, N.Delcour, J.Alvarez, A.Cortes, A.Willis, C.Holbrook, J.J.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
D-LACTATE DEHYDROGENASE
A, B
337Lactobacillus helveticusMutation(s): 0 
EC: 1.1.1.28
UniProt
Find proteins for P30901 (Lactobacillus helveticus)
Explore P30901 
Go to UniProtKB:  P30901
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP30901
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.297 
  • R-Value Observed: 0.195 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 86.2α = 90
b = 62.1β = 113.2
c = 77.4γ = 90
Software Package:
Software NamePurpose
PROLSQrefinement
XENGENdata reduction

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-03-14
    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: 2013-11-06
    Changes: Non-polymer description