5LOC

Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.04 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.209 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history. 


Literature

Single-biocatalyst synthesis of enantiopure D-arylalanines exploiting an engineered D-amino acid dehydrogenase

Parmeggiani, F., Ahmed, S.T., Thompson, M.P., Weise, N.J., Galman, J.L., Gahloth, D., Dunstan, M.S., Leys, D., Turner, N.J.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Meso-diaminopimelate D-dehydrogenase
A, B
320Corynebacterium glutamicumMutation(s): 0 
Gene Names: ddh, Cgl2617, cg2900
EC: 1.4.1.16
UniProt
Find proteins for P04964 (Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025))
Explore P04964 
Go to UniProtKB:  P04964
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04964
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.04 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.209 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 120.53α = 90
b = 120.53β = 90
c = 97.63γ = 120
Software Package:
Software NamePurpose
xia2data scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
XDSdata reduction
PHASERphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-08-16
    Type: Initial release
  • Version 1.1: 2019-10-16
    Changes: Data collection