Manganese in PDB 4rcv: M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase Bound to 1-Deoxy-L-Erythrulose

All present enzymatic activity of M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase Bound to 1-Deoxy-L-Erythrulose:
1.1.1.267;

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

Resolution Low / High (Å)	35.16 / 2.29
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.370, 64.378, 85.741, 90.00, 101.73, 90.00
R / Rfree (%)	17.3 / 23.2

The binding sites of Manganese atom in the M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase Bound to 1-Deoxy-L-Erythrulose (pdb code 4rcv). 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 Bound to 1-Deoxy-L-Erythrulose, PDB code: 4rcv:
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 Bound to 1-Deoxy-L-Erythrulose


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 Bound to 1-Deoxy-L-Erythrulose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:33.7 occ:1.00 OD1 A:ASP151 2.1 32.1 1.0 OE2 A:GLU222 2.2 24.3 1.0 OE2 A:GLU153 2.2 21.6 1.0 O5 A:DE2403 2.4 27.3 1.0 O3 A:DE2403 2.5 23.5 1.0 O2 A:DE2403 2.5 30.1 1.0 C3 A:DE2403 2.9 35.1 1.0 CD A:GLU153 3.0 24.0 1.0 CG A:ASP151 3.1 27.6 1.0 C2 A:DE2403 3.1 31.8 1.0 C4 A:DE2403 3.1 28.3 1.0 CD A:GLU222 3.2 18.9 1.0 OE1 A:GLU153 3.2 24.7 1.0 OD2 A:ASP151 3.5 23.6 1.0 OE1 A:GLU222 3.7 23.2 1.0 NZ A:LYS128 3.8 27.4 1.0 C5N A:NDP402 4.1 27.6 1.0 N A:SER152 4.1 23.4 1.0 ND2 A:ASN218 4.2 22.2 1.0 CG A:GLU222 4.3 14.8 1.0 CB A:ASP151 4.3 24.6 1.0 CG A:GLU153 4.4 18.9 1.0 C1 A:DE2403 4.5 31.6 1.0 N A:GLU153 4.5 20.2 1.0 CA A:ASP151 4.6 20.3 1.0 C A:ASP151 4.7 25.5 1.0 NZ A:LYS219 4.8 15.5 1.0 CB A:SER152 4.8 19.7 1.0 C6N A:NDP402 4.8 29.1 1.0 CB A:GLU153 4.9 16.9 1.0 CA A:SER152 4.9 22.7 1.0 C4N A:NDP402 5.0 29.1 1.0

Manganese binding site 2 out of 2 in the M. Tuberculosis 1-Deoxy-D-Xylulose-5-Phosphate Reductoisomerase Bound to 1-Deoxy-L-Erythrulose


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 Bound to 1-Deoxy-L-Erythrulose within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:52.1 occ:1.00 OE2 B:GLU222 2.2 35.1 1.0 OE2 B:GLU153 2.2 26.2 1.0 OD1 B:ASP151 2.2 38.0 1.0 CG B:ASP151 2.9 34.8 1.0 OD2 B:ASP151 3.0 34.1 1.0 CD B:GLU222 3.1 31.0 1.0 CD B:GLU153 3.3 29.2 1.0 OE1 B:GLU222 3.5 26.8 1.0 OE1 B:GLU153 3.9 40.9 1.0 OG B:SER152 4.2 32.3 1.0 CG B:GLU222 4.3 23.5 1.0 CB B:ASP151 4.4 23.9 1.0 N B:SER152 4.4 24.1 1.0 ND2 B:ASN218 4.4 42.9 1.0 N B:GLU153 4.4 20.4 1.0 CG B:GLU153 4.5 23.1 1.0 CB B:GLU153 4.6 26.4 1.0 O3 B:PO3403 4.6 46.6 1.0 CA B:ASP151 5.0 23.4 1.0

S.A.Kholodar, C.L.Allen, A.M.Gulick, A.S.Murkin. The Role of Phosphate in A Multistep Enzymatic Reaction: Reactions of the Substrate and Intermediate in Pieces. J.Am.Chem.Soc. V. 137 2748 2015.
ISSN: ISSN 0002-7863
PubMed: 25642788
DOI: 10.1021/JA512911F