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3HA1

Alanine racemase from Bacillus Anthracis (Ames)

Summary for 3HA1
Entry DOI10.2210/pdb3ha1/pdb
Related1rcq 1sft 1xfc 2vd8
DescriptorAlanine racemase, ACETATE ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsalanine racemase, isomerase, plp, pyridoxal phosphate
Biological sourceBacillus anthracis (anthrax,anthrax bacterium)
Total number of polymer chains2
Total formula weight90139.35
Authors
Counago, R.M.,Davlieva, M.,Strych, U.,Hill, R.E.,Krause, K.L. (deposition date: 2009-04-30, release date: 2009-09-15, Last modification date: 2023-11-22)
Primary citationCounago, R.M.,Davlieva, M.,Strych, U.,Hill, R.E.,Krause, K.L.
Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames).
Bmc Struct.Biol., 9:53-53, 2009
Cited by
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.
PubMed: 19695097
DOI: 10.1186/1472-6807-9-53
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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