Iron in PDB 8czp: 2.25 Angstrom Resolution Crystal Structure of As-Isolated Katg From Mycobacterium Tuberculosis with An Myw Cofactor

All present enzymatic activity of 2.25 Angstrom Resolution Crystal Structure of As-Isolated Katg From Mycobacterium Tuberculosis with An Myw Cofactor:
1.11.1.21;

The structure of 2.25 Angstrom Resolution Crystal Structure of As-Isolated Katg From Mycobacterium Tuberculosis with An Myw Cofactor, PDB code: 8czp was solved by J.Li, A.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.68 / 2.25
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	150.699, 150.699, 155.491, 90, 90, 90
R / Rfree (%)	24 / 28.3

The binding sites of Iron atom in the 2.25 Angstrom Resolution Crystal Structure of As-Isolated Katg From Mycobacterium Tuberculosis with An Myw Cofactor (pdb code 8czp). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the 2.25 Angstrom Resolution Crystal Structure of As-Isolated Katg From Mycobacterium Tuberculosis with An Myw Cofactor, PDB code: 8czp:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the 2.25 Angstrom Resolution Crystal Structure of As-Isolated Katg From Mycobacterium Tuberculosis with An Myw Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 2.25 Angstrom Resolution Crystal Structure of As-Isolated Katg From Mycobacterium Tuberculosis with An Myw Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1500 b:26.9 occ:1.00 FE A:HEM1500 0.0 26.9 1.0 NC A:HEM1500 2.0 26.8 1.0 NA A:HEM1500 2.0 27.8 1.0 ND A:HEM1500 2.0 28.6 1.0 NB A:HEM1500 2.0 25.5 1.0 NE2 A:HIS270 2.3 25.6 1.0 O A:HOH1739 2.7 30.1 1.0 C4C A:HEM1500 3.0 26.0 1.0 C4A A:HEM1500 3.0 27.6 1.0 C1D A:HEM1500 3.0 27.2 1.0 C1C A:HEM1500 3.0 24.1 1.0 C1B A:HEM1500 3.0 24.3 1.0 C4D A:HEM1500 3.1 31.6 1.0 C4B A:HEM1500 3.1 25.6 1.0 C1A A:HEM1500 3.1 25.8 1.0 CD2 A:HIS270 3.2 25.8 1.0 CE1 A:HIS270 3.3 27.6 1.0 CHD A:HEM1500 3.4 23.1 1.0 CHB A:HEM1500 3.4 24.7 1.0 CHC A:HEM1500 3.5 27.8 1.0 CHA A:HEM1500 3.5 25.6 1.0 NE1 A:TRP107 4.2 21.2 1.0 C2D A:HEM1500 4.2 26.0 1.0 C3C A:HEM1500 4.2 28.2 1.0 C3A A:HEM1500 4.2 28.1 1.0 C2C A:HEM1500 4.2 23.6 1.0 C3D A:HEM1500 4.3 28.9 1.0 C2B A:HEM1500 4.3 26.5 1.0 C2A A:HEM1500 4.3 26.6 1.0 C3B A:HEM1500 4.3 22.1 1.0 CG A:HIS270 4.4 24.9 1.0 O A:HOH1715 4.4 28.9 1.0 ND1 A:HIS270 4.4 27.5 1.0 CD1 A:TRP107 4.5 20.9 1.0 CH2 A:TRP321 4.8 25.4 1.0

Iron binding site 2 out of 2 in the 2.25 Angstrom Resolution Crystal Structure of As-Isolated Katg From Mycobacterium Tuberculosis with An Myw Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 2.25 Angstrom Resolution Crystal Structure of As-Isolated Katg From Mycobacterium Tuberculosis with An Myw Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:25.6 occ:1.00 FE B:HEM801 0.0 25.6 1.0 NC B:HEM801 1.9 18.5 1.0 NA B:HEM801 1.9 17.7 1.0 ND B:HEM801 2.0 25.5 1.0 NB B:HEM801 2.1 21.3 1.0 NE2 B:HIS270 2.4 21.7 1.0 O B:HOH1033 2.5 20.9 1.0 C1A B:HEM801 2.9 17.2 1.0 C4C B:HEM801 2.9 19.6 1.0 C1C B:HEM801 3.0 19.2 1.0 C4D B:HEM801 3.0 16.9 1.0 C1D B:HEM801 3.0 18.0 1.0 C4A B:HEM801 3.0 14.4 1.0 C4B B:HEM801 3.1 16.1 1.0 C1B B:HEM801 3.1 13.5 1.0 CD2 B:HIS270 3.2 18.3 1.0 CHA B:HEM801 3.3 18.1 1.0 CHD B:HEM801 3.4 17.3 1.0 CHC B:HEM801 3.4 16.9 1.0 CHB B:HEM801 3.5 15.3 1.0 CE1 B:HIS270 3.5 14.6 1.0 O B:HOH908 3.7 21.9 1.0 C2A B:HEM801 4.1 14.4 1.0 C3C B:HEM801 4.2 16.4 1.0 C2C B:HEM801 4.2 18.1 1.0 C3A B:HEM801 4.2 12.9 1.0 C2D B:HEM801 4.2 15.3 1.0 C3D B:HEM801 4.2 17.8 1.0 C3B B:HEM801 4.3 16.6 1.0 C2B B:HEM801 4.3 14.9 1.0 CG B:HIS270 4.4 22.7 1.0 NE1 B:TRP107 4.5 22.2 1.0 ND1 B:HIS270 4.5 22.1 1.0 CD1 B:TRP107 4.7 18.9 1.0 CH2 B:TRP321 4.8 21.6 1.0

J.Li, A.Liu. 2.25 Angstrom Resolution Crystal Structure of As-Isolated Katg From Mycobacterium Tuberculosis with An Myw Cofactor To Be Published.