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4C51

Crystal Structure of the Catalase-Peroxidase (KatG) R418L mutant from Mycobacterium Tuberculosis

Summary for 4C51
Entry DOI10.2210/pdb4c51/pdb
Related4C50
DescriptorCATALASE-PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE, alpha-D-glucopyranose, ... (4 entities in total)
Functional Keywordsoxidoreductase
Biological sourceMYCOBACTERIUM TUBERCULOSIS H37RV
Total number of polymer chains2
Total formula weight162880.43
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 citationZhao, 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: 24185282
DOI: 10.1039/C3CC47022A
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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