5TI8

Crystal Structure of an aspartate aminotransferase from Pseudomonas


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.07 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.187 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC.

Wilding, M.Scott, C.Newman, J.Peat, T.S.

(2017) Acta Crystallogr F Struct Biol Commun 73: 29-35

  • DOI: https://doi.org/10.1107/S2053230X16019658
  • Primary Citation of Related Structures:  
    5TI8

  • PubMed Abstract: 

    The putrescine aminotransferase KES24511 from Pseudomonas sp. strain AAC was previously identified as an industrially relevant enzyme based on the discovery that it is able to promiscuously catalyse the transamination of 12-aminododecanoic acid. Here, the cloning, heterologous expression, purification and successful crystallization of the KES24511 protein are reported, which ultimately generated crystals adopting space group I2. The crystals diffracted X-rays to 2.07 Å resolution and data were collected using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4a6t as the search model.


  • Organizational Affiliation

    Land and Water, CSIRO, GPO Box 1700, Canberra, ACT 2601, Australia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Aminotransferase
A, B
474Pseudomonas sp. M1Mutation(s): 0 
Gene Names: PM1_0202430
UniProt
Find proteins for W5IS25 (Pseudomonas sp. (strain M1))
Explore W5IS25 
Go to UniProtKB:  W5IS25
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupW5IS25
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.07 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.187 
  • Space Group: I 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.444α = 90
b = 95.429β = 100.21
c = 114.449γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-01-11
    Type: Initial release
  • Version 1.1: 2023-10-04
    Changes: Data collection, Database references, Derived calculations, Refinement description