Manganese in PDB 4oof: M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase W203F Mutant Bound to Fosmidomycin and Nadph

All present enzymatic activity of M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase W203F Mutant Bound to Fosmidomycin and Nadph:
1.1.1.267;

The structure of M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase W203F Mutant Bound to Fosmidomycin and Nadph, PDB code: 4oof was solved by C.L.Allen, S.A.Kholodar, A.S.Murkin, A.M.Gulick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.78 / 2.30
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	107.912, 107.912, 136.438, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 21.2

The binding sites of Manganese atom in the M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase W203F Mutant Bound to Fosmidomycin and Nadph (pdb code 4oof). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase W203F Mutant Bound to Fosmidomycin and Nadph, PDB code: 4oof:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase W203F Mutant Bound to Fosmidomycin and Nadph


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase W203F Mutant Bound to Fosmidomycin and Nadph within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:23.2 occ:1.00 O2 A:FOM402 2.0 21.1 1.0 OE1 A:GLU153 2.0 22.4 1.0 OD1 A:ASP151 2.1 27.2 1.0 OE2 A:GLU222 2.1 24.7 1.0 O1 A:FOM402 2.2 26.1 1.0 N1 A:FOM402 2.8 23.8 1.0 CD A:GLU153 2.8 25.2 1.0 C1 A:FOM402 2.9 26.0 1.0 CD A:GLU222 3.0 28.8 1.0 OE2 A:GLU153 3.0 24.9 1.0 CG A:ASP151 3.0 26.3 1.0 OE1 A:GLU222 3.4 27.6 1.0 OD2 A:ASP151 3.5 28.5 1.0 NZ A:LYS128 3.7 23.8 1.0 N A:SER152 4.0 24.5 1.0 C5N A:NDP400 4.0 27.5 1.0 CG A:GLU222 4.2 21.8 1.0 OG A:SER152 4.2 23.8 1.0 ND2 A:ASN218 4.2 23.2 1.0 C2 A:FOM402 4.2 23.3 1.0 CG A:GLU153 4.3 20.1 1.0 CB A:ASP151 4.3 23.2 1.0 N A:GLU153 4.4 22.7 1.0 C3 A:FOM402 4.5 27.0 1.0 CA A:ASP151 4.6 25.0 1.0 C A:ASP151 4.6 23.2 1.0 CB A:GLU153 4.8 21.2 1.0 C4 A:FOM402 4.8 25.1 1.0 C4N A:NDP400 4.8 28.8 1.0 CA A:SER152 4.8 25.9 1.0 C6N A:NDP400 4.9 24.1 1.0 CB A:SER152 4.9 23.5 1.0 NZ A:LYS219 4.9 22.8 1.0 CE A:LYS128 5.0 26.5 1.0

Manganese binding site 2 out of 2 in the M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase W203F Mutant Bound to Fosmidomycin and Nadph


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase W203F Mutant Bound to Fosmidomycin and Nadph within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:25.6 occ:1.00 OD1 B:ASP151 2.0 29.3 1.0 O2 B:FOM402 2.0 25.1 1.0 OE2 B:GLU222 2.0 23.4 1.0 OE1 B:GLU153 2.1 25.6 1.0 O1 B:FOM402 2.2 22.9 1.0 N1 B:FOM402 2.8 27.0 1.0 C1 B:FOM402 2.8 26.6 1.0 CD B:GLU153 2.9 26.0 1.0 CG B:ASP151 3.0 25.8 1.0 OE2 B:GLU153 3.0 28.5 1.0 CD B:GLU222 3.0 26.2 1.0 OD2 B:ASP151 3.4 29.3 1.0 OE1 B:GLU222 3.5 21.5 1.0 NZ B:LYS128 3.8 28.6 1.0 N B:SER152 3.9 27.6 1.0 C5N B:NDP400 4.0 25.9 1.0 OG B:SER152 4.1 22.5 1.0 CG B:GLU222 4.2 25.2 1.0 CB B:ASP151 4.2 27.5 1.0 C2 B:FOM402 4.2 26.1 1.0 ND2 B:ASN218 4.3 25.6 1.0 CG B:GLU153 4.3 24.3 1.0 N B:GLU153 4.3 21.9 1.0 CA B:ASP151 4.5 25.3 1.0 C B:ASP151 4.5 25.9 1.0 C3 B:FOM402 4.7 25.5 1.0 C6N B:NDP400 4.7 25.9 1.0 NZ B:LYS219 4.8 23.6 1.0 CB B:GLU153 4.8 24.8 1.0 C4 B:FOM402 4.8 22.9 1.0 CA B:SER152 4.8 24.9 1.0 C4N B:NDP400 4.8 27.1 1.0 CB B:SER152 4.9 24.7 1.0 OD1 B:ASN218 5.0 23.3 1.0

S.A.Kholodar, G.Tombline, J.Liu, Z.Tan, C.L.Allen, A.M.Gulick, A.S.Murkin. Alteration of the Flexible Loop in 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase Boosts Enthalpy-Driven Inhibition By Fosmidomycin. Biochemistry V. 53 3423 2014.
ISSN: ISSN 0006-2960
PubMed: 24825256
DOI: 10.1021/BI5004074