Iron in PDB 4c50: Crystal Structure of the Catalase-Peroxidase (Katg) D137S Mutant From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure of the Catalase-Peroxidase (Katg) D137S Mutant From Mycobacterium Tuberculosis:
1.11.1.21;

The structure of Crystal Structure of the Catalase-Peroxidase (Katg) D137S Mutant From Mycobacterium Tuberculosis, PDB code: 4c50 was solved by H.-P.Hersleth, X.Zhao, R.S.Magliozzo, K.K.Andersson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	75.41 / 2.50
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	150.590, 150.590, 157.350, 90.00, 90.00, 90.00
R / Rfree (%)	26.363 / 31.113

The binding sites of Iron atom in the Crystal Structure of the Catalase-Peroxidase (Katg) D137S Mutant From Mycobacterium Tuberculosis (pdb code 4c50). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Catalase-Peroxidase (Katg) D137S Mutant From Mycobacterium Tuberculosis, PDB code: 4c50:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Catalase-Peroxidase (Katg) D137S Mutant From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the Catalase-Peroxidase (Katg) D137S Mutant From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1741 b:23.1 occ:1.00 FE A:HEM1741 0.0 23.1 1.0 NA A:HEM1741 1.8 21.7 1.0 NC A:HEM1741 1.8 21.1 1.0 NB A:HEM1741 2.0 21.0 1.0 NE2 A:HIS270 2.1 28.4 1.0 ND A:HEM1741 2.2 22.0 1.0 O A:HOH2007 2.8 20.3 1.0 C1C A:HEM1741 2.8 21.7 1.0 C1A A:HEM1741 2.9 22.4 1.0 C4A A:HEM1741 2.9 22.2 1.0 C4C A:HEM1741 2.9 22.2 1.0 C4B A:HEM1741 3.0 20.1 1.0 CD2 A:HIS270 3.0 29.2 1.0 C1B A:HEM1741 3.1 21.3 1.0 C4D A:HEM1741 3.1 21.5 1.0 C1D A:HEM1741 3.2 21.6 1.0 CE1 A:HIS270 3.2 29.2 1.0 CHC A:HEM1741 3.3 20.7 1.0 CHA A:HEM1741 3.4 21.4 1.0 CHB A:HEM1741 3.4 21.3 1.0 CHD A:HEM1741 3.4 22.2 1.0 C2A A:HEM1741 4.1 23.9 1.0 C3A A:HEM1741 4.1 22.5 1.0 C2C A:HEM1741 4.1 21.6 1.0 C3C A:HEM1741 4.1 20.8 1.0 CG A:HIS270 4.2 28.8 1.0 C3B A:HEM1741 4.2 21.2 1.0 C2B A:HEM1741 4.2 22.0 1.0 ND1 A:HIS270 4.3 28.6 1.0 NE1 A:TRP107 4.3 22.4 1.0 C2D A:HEM1741 4.4 21.6 1.0 C3D A:HEM1741 4.4 21.9 1.0 CD1 A:TRP107 4.7 22.0 1.0 O A:HOH2008 4.9 15.4 1.0 CH2 A:TRP321 5.0 37.0 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Catalase-Peroxidase (Katg) D137S Mutant From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Catalase-Peroxidase (Katg) D137S Mutant From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1741 b:26.2 occ:1.00 FE B:HEM1741 0.0 26.2 1.0 NC B:HEM1741 1.8 27.8 1.0 NB B:HEM1741 2.0 29.6 1.0 NA B:HEM1741 2.1 27.5 1.0 NE2 B:HIS270 2.1 28.3 1.0 ND B:HEM1741 2.2 25.4 1.0 C4C B:HEM1741 2.8 27.0 1.0 CD2 B:HIS270 2.9 29.5 1.0 C1C B:HEM1741 2.9 29.7 1.0 C1B B:HEM1741 3.0 31.3 1.0 C4A B:HEM1741 3.0 29.1 1.0 O B:HOH2008 3.0 25.6 1.0 C1D B:HEM1741 3.1 24.3 1.0 C4B B:HEM1741 3.1 31.2 1.0 C1A B:HEM1741 3.2 28.1 1.0 CE1 B:HIS270 3.2 28.8 1.0 C4D B:HEM1741 3.3 25.6 1.0 CHD B:HEM1741 3.3 24.8 1.0 CHB B:HEM1741 3.3 29.9 1.0 CHC B:HEM1741 3.5 31.5 1.0 CHA B:HEM1741 3.7 26.8 1.0 C3C B:HEM1741 4.1 28.4 1.0 C2C B:HEM1741 4.1 28.3 1.0 CG B:HIS270 4.2 29.4 1.0 C2B B:HEM1741 4.2 33.6 1.0 C3B B:HEM1741 4.2 32.6 1.0 C3A B:HEM1741 4.3 30.2 1.0 NE1 B:TRP107 4.3 25.5 1.0 ND1 B:HIS270 4.3 29.1 1.0 C2D B:HEM1741 4.3 23.7 1.0 C2A B:HEM1741 4.4 29.5 1.0 C3D B:HEM1741 4.4 23.3 1.0 O B:HOH2009 4.5 21.2 1.0 CD1 B:TRP107 4.6 24.2 1.0 CH2 B:TRP321 4.9 40.1 1.0

X.Zhao, H.P.Hersleth, J.Zhu, K.K.Andersson, R.S.Magliozzo. Access Channel Residues SER315 and ASP137 in Mycobacterium Tuberculosis Catalase-Peroxidase (Katg) Control Peroxidatic Activation of the Pro-Drug Isoniazid. Chem.Commun.(Camb.) V. 49 11650 2013.
ISSN: ISSN 1359-7345
PubMed: 24185282
DOI: 10.1039/C3CC47022A