3HA1
Alanine racemase from Bacillus Anthracis (Ames)
Summary for 3HA1
| Entry DOI | 10.2210/pdb3ha1/pdb |
| Related | 1rcq 1sft 1xfc 2vd8 |
| Descriptor | Alanine racemase, ACETATE ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | alanine racemase, isomerase, plp, pyridoxal phosphate |
| Biological source | Bacillus anthracis (anthrax,anthrax bacterium) |
| Total number of polymer chains | 2 |
| Total formula weight | 90139.35 |
| 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 citation | Counago, 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: 19695097DOI: 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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