Iron in PDB 7ag8: Cryo-Em Structure of Wild-Type Katg From M. Tuberculosis

All present enzymatic activity of Cryo-Em Structure of Wild-Type Katg From M. Tuberculosis:
1.11.1.21;

The binding sites of Iron atom in the Cryo-Em Structure of Wild-Type Katg From M. Tuberculosis (pdb code 7ag8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cryo-Em Structure of Wild-Type Katg From M. Tuberculosis, PDB code: 7ag8:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cryo-Em Structure of Wild-Type Katg From M. Tuberculosis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of Wild-Type Katg From M. Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:93.9 occ:1.00 FE A:HEM801 0.0 93.9 1.0 NA A:HEM801 2.0 93.9 1.0 ND A:HEM801 2.0 93.9 1.0 NC A:HEM801 2.0 93.9 1.0 NB A:HEM801 2.0 93.9 1.0 NE2 A:HIS270 2.6 101.3 1.0 C4C A:HEM801 3.0 93.9 1.0 C1C A:HEM801 3.0 93.9 1.0 C4A A:HEM801 3.0 93.9 1.0 C1A A:HEM801 3.0 93.9 1.0 C1D A:HEM801 3.0 93.9 1.0 C4D A:HEM801 3.0 93.9 1.0 C4B A:HEM801 3.1 93.9 1.0 C1B A:HEM801 3.1 93.9 1.0 CD2 A:HIS270 3.3 101.3 1.0 CHA A:HEM801 3.4 93.9 1.0 CHD A:HEM801 3.4 93.9 1.0 CHC A:HEM801 3.4 93.9 1.0 CHB A:HEM801 3.4 93.9 1.0 CE1 A:HIS270 3.8 101.3 1.0 NE1 A:TRP107 3.9 83.7 1.0 CZ2 A:TRP107 3.9 83.7 1.0 CE2 A:TRP107 4.2 83.7 1.0 C2C A:HEM801 4.2 93.9 1.0 C3C A:HEM801 4.2 93.9 1.0 C3A A:HEM801 4.2 93.9 1.0 C2A A:HEM801 4.2 93.9 1.0 C2D A:HEM801 4.2 93.9 1.0 C3D A:HEM801 4.3 93.9 1.0 C2B A:HEM801 4.3 93.9 1.0 C3B A:HEM801 4.3 93.9 1.0 CG A:HIS270 4.5 101.3 1.0 ND1 A:HIS270 4.8 101.3 1.0 CD1 A:TRP107 5.0 83.7 1.0

Iron binding site 2 out of 2 in the Cryo-Em Structure of Wild-Type Katg From M. Tuberculosis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of Wild-Type Katg From M. Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:104.0 occ:1.00 FE B:HEM801 0.0 104.0 1.0 NA B:HEM801 2.0 104.0 1.0 NB B:HEM801 2.0 104.0 1.0 ND B:HEM801 2.0 104.0 1.0 NC B:HEM801 2.1 104.0 1.0 NE2 B:HIS270 2.6 92.7 1.0 C4B B:HEM801 3.0 104.0 1.0 C1B B:HEM801 3.0 104.0 1.0 C4A B:HEM801 3.0 104.0 1.0 C1A B:HEM801 3.0 104.0 1.0 C1D B:HEM801 3.1 104.0 1.0 C1C B:HEM801 3.1 104.0 1.0 C4D B:HEM801 3.1 104.0 1.0 C4C B:HEM801 3.1 104.0 1.0 CD2 B:HIS270 3.2 92.7 1.0 CZ2 B:TRP107 3.2 105.4 1.0 CHC B:HEM801 3.4 104.0 1.0 CHB B:HEM801 3.4 104.0 1.0 CHA B:HEM801 3.4 104.0 1.0 CHD B:HEM801 3.4 104.0 1.0 CE1 B:HIS270 3.8 92.7 1.0 CE2 B:TRP107 3.9 105.4 1.0 CH2 B:TRP107 4.1 105.4 1.0 NE1 B:TRP107 4.1 105.4 1.0 C3B B:HEM801 4.2 104.0 1.0 C2B B:HEM801 4.2 104.0 1.0 C3A B:HEM801 4.3 104.0 1.0 C2A B:HEM801 4.3 104.0 1.0 C2D B:HEM801 4.3 104.0 1.0 C3D B:HEM801 4.3 104.0 1.0 C2C B:HEM801 4.3 104.0 1.0 C3C B:HEM801 4.3 104.0 1.0 CG B:HIS270 4.5 92.7 1.0 ND1 B:HIS270 4.7 92.7 1.0

A.Munir, M.T.Wilson, S.W.Hardwick, D.Y.Chirgadze, J.A.R.Worrall, T.L.Blundell, A.K.Chaplin. Using Cryo-Em to Understand Antimycobacterial Resistance in the Catalase-Peroxidase (Katg) From Mycobacterium Tuberculosis. Structure 2021.
ISSN: ISSN 0969-2126
PubMed: 33444527
DOI: 10.1016/J.STR.2020.12.008