Iron in PDB 7a2i: Cryo-Em Structure of W107R Katg From M. Tuberculosis

Enzymatic activity of Cryo-Em Structure of W107R Katg From M. Tuberculosis

All present enzymatic activity of Cryo-Em Structure of W107R Katg From M. Tuberculosis:
1.11.1.21;

Iron Binding Sites:

The binding sites of Iron atom in the Cryo-Em Structure of W107R Katg From M. Tuberculosis (pdb code 7a2i). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Cryo-Em Structure of W107R Katg From M. Tuberculosis, PDB code: 7a2i:

Iron binding site 1 out of 1 in 7a2i

Go back to Iron Binding Sites List in 7a2i
Iron binding site 1 out of 1 in the Cryo-Em Structure of W107R 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 W107R Katg From M. Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe801

b:95.0
occ:1.00
FE B:HEM801 0.0 95.0 1.0
ND B:HEM801 2.0 95.0 1.0
NC B:HEM801 2.0 95.0 1.0
NB B:HEM801 2.0 95.0 1.0
NA B:HEM801 2.0 95.0 1.0
NE2 B:HIS270 2.8 85.8 1.0
CE1 B:HIS270 2.9 85.8 1.0
C1C B:HEM801 3.0 95.0 1.0
C1D B:HEM801 3.0 95.0 1.0
C4D B:HEM801 3.1 95.0 1.0
C4B B:HEM801 3.1 95.0 1.0
C4C B:HEM801 3.1 95.0 1.0
C1A B:HEM801 3.1 95.0 1.0
C4A B:HEM801 3.1 95.0 1.0
C1B B:HEM801 3.1 95.0 1.0
CHC B:HEM801 3.4 95.0 1.0
CHD B:HEM801 3.4 95.0 1.0
CHA B:HEM801 3.4 95.0 1.0
CHB B:HEM801 3.4 95.0 1.0
CD2 B:HIS270 3.8 85.8 1.0
ND1 B:HIS270 3.9 85.8 1.0
C2C B:HEM801 4.2 95.0 1.0
C2D B:HEM801 4.3 95.0 1.0
C3D B:HEM801 4.3 95.0 1.0
C3C B:HEM801 4.3 95.0 1.0
C3A B:HEM801 4.3 95.0 1.0
C3B B:HEM801 4.3 95.0 1.0
C2A B:HEM801 4.3 95.0 1.0
C2B B:HEM801 4.3 95.0 1.0
CG B:HIS270 4.4 85.8 1.0

Reference:

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
Page generated: Wed Mar 3 14:01:12 2021

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