3HA1

Alanine racemase from Bacillus Anthracis (Ames)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.201 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.161 

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This is version 1.3 of the entry. See complete history. 


Literature

Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames).

Counago, R.M., Davlieva, M., Strych, U., Hill, R.E., Krause, K.L.

(2009) BMC Struct Biol 9: 53-53

  • DOI: https://doi.org/10.1186/1472-6807-9-53
  • Primary Citation of Related Structures:  
    3HA1

  • PubMed Abstract: 

    Bacillus anthracis is the causative agent of anthrax and a potential bioterrorism threat. Here we report the biochemical and structural characterization of B. anthracis (Ames) alanine racemase (AlrBax), an essential enzyme in prokaryotes and a target for antimicrobial drug development. We also compare the native AlrBax structure to a recently reported structure of the same enzyme obtained through reductive lysine methylation.

    • Organizational Affiliation: 

    Department of Biochemistry, University of Otago, Dunedin, New Zealand. rafael.counago@otago.ac.nz


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Alanine racemase
A, B
397Bacillus anthracisMutation(s): 0 
Gene Names: dal-1, dal1
EC: 5.1.1.1
UniProt
Find proteins for A0A6L7HC45 (Bacillus anthracis)
Explore A0A6L7HC45 
Go to UniProtKB:  A0A6L7HC45
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A6L7HC45
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.201 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.161 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.624α = 90
b = 141.271β = 103.11
c = 60.124γ = 90
Software Package:
Software NamePurpose
SCALAdata scaling
REFMACrefinement
PDB_EXTRACTdata extraction
CrystalCleardata collection
MOSFLMdata reduction
MOLREPphasing

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: 2009-09-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.3: 2023-11-22
    Changes: Data collection