4C51
Crystal Structure of the Catalase-Peroxidase (KatG) R418L mutant from Mycobacterium Tuberculosis
Summary for 4C51
Entry DOI | 10.2210/pdb4c51/pdb |
Related | 4C50 |
Descriptor | CATALASE-PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE, alpha-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | oxidoreductase |
Biological source | MYCOBACTERIUM TUBERCULOSIS H37RV |
Total number of polymer chains | 2 |
Total formula weight | 162880.43 |
Authors | Hersleth, H.-P.,Zhao, X.,Magliozzo, R.S.,Andersson, K.K. (deposition date: 2013-09-10, release date: 2013-11-13, Last modification date: 2023-12-20) |
Primary citation | Zhao, X.,Hersleth, H.P.,Zhu, J.,Andersson, K.K.,Magliozzo, R.S. Access Channel Residues Ser315 and Asp137 in Mycobacterium Tuberculosis Catalase-Peroxidase (Katg) Control Peroxidatic Activation of the Pro-Drug Isoniazid. Chem.Commun.(Camb.), 49:11650-, 2013 Cited by PubMed Abstract: Peroxidatic activation of the anti-tuberculosis pro-drug isoniazid by Mycobacterium tuberculosis catalase-peroxidase (KatG) is regulated by gating residues of a heme access channel. The steric restriction at the bottleneck of this channel is alleviated by replacement of residue Asp137 with Ser, according to crystallographic and kinetic studies. PubMed: 24185282DOI: 10.1039/C3CC47022A PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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