Manganese in PDB 1onp: Ispc Complex with MN2+ and Fosmidomycin

All present enzymatic activity of Ispc Complex with MN2+ and Fosmidomycin:
1.1.1.267;

The structure of Ispc Complex with MN2+ and Fosmidomycin, PDB code: 1onp was solved by S.Steinbacher, J.Kaiser, W.Eisenreich, R.Huber, A.Bacher, F.Rohdich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	90.754, 52.301, 107.595, 90.00, 92.11, 90.00
R / Rfree (%)	25.5 / 33

The binding sites of Manganese atom in the Ispc Complex with MN2+ and Fosmidomycin (pdb code 1onp). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Ispc Complex with MN2+ and Fosmidomycin, PDB code: 1onp:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Ispc Complex with MN2+ and Fosmidomycin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Ispc Complex with MN2+ and Fosmidomycin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1002 b:67.0 occ:1.00 O2 A:FOM1001 2.1 77.1 1.0 OE1 A:GLU231 2.2 53.2 1.0 OD2 A:ASP150 2.2 59.4 1.0 O A:HOH1085 2.2 73.4 1.0 OE2 A:GLU152 2.2 61.9 1.0 O1 A:FOM1001 2.4 56.9 1.0 N1 A:FOM1001 2.9 75.4 1.0 C1 A:FOM1001 2.9 69.3 1.0 CG A:ASP150 2.9 51.8 1.0 OD1 A:ASP150 3.3 58.4 1.0 CD A:GLU231 3.3 52.0 1.0 CD A:GLU152 3.5 56.5 1.0 OE2 A:GLU231 4.0 52.6 1.0 CB A:ASP150 4.1 51.8 1.0 OE1 A:GLU152 4.2 53.8 1.0 N A:SER151 4.2 49.6 1.0 N A:GLU152 4.3 41.8 1.0 C2 A:FOM1001 4.3 78.0 1.0 CG A:GLU231 4.4 52.7 1.0 CB A:GLU152 4.6 43.4 1.0 CG A:GLU152 4.6 51.5 1.0 CA A:ASP150 4.6 48.5 1.0 C A:ASP150 4.6 49.5 1.0 CB A:SER151 4.7 49.6 1.0 CA A:SER151 4.9 47.0 1.0 ND2 A:ASN227 4.9 59.3 1.0 C3 A:FOM1001 5.0 76.5 1.0

Manganese binding site 2 out of 2 in the Ispc Complex with MN2+ and Fosmidomycin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Ispc Complex with MN2+ and Fosmidomycin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1002 b:62.4 occ:1.00 O2 B:FOM1001 2.1 73.3 1.0 OE1 B:GLU231 2.2 56.1 1.0 OD2 B:ASP150 2.2 58.7 1.0 O B:HOH1064 2.2 62.6 1.0 OE2 B:GLU152 2.2 60.9 1.0 O1 B:FOM1001 2.3 64.4 1.0 C1 B:FOM1001 2.8 71.6 1.0 N1 B:FOM1001 2.8 73.7 1.0 CG B:ASP150 2.9 52.7 1.0 OD1 B:ASP150 3.2 61.8 1.0 CD B:GLU231 3.4 52.7 1.0 CD B:GLU152 3.5 55.6 1.0 OE2 B:GLU231 4.1 50.9 1.0 OE1 B:GLU152 4.1 54.4 1.0 N B:SER151 4.2 47.2 1.0 CB B:ASP150 4.2 47.2 1.0 C2 B:FOM1001 4.3 77.2 1.0 N B:GLU152 4.3 41.5 1.0 CB B:SER151 4.5 48.6 1.0 CG B:GLU231 4.5 52.4 1.0 C B:ASP150 4.6 48.0 1.0 CG B:GLU152 4.6 48.3 1.0 CB B:GLU152 4.6 41.9 1.0 CA B:ASP150 4.6 44.2 1.0 CA B:SER151 4.8 44.2 1.0 C3 B:FOM1001 4.9 79.7 1.0 O B:HOH1010 4.9 39.6 1.0 ND2 B:ASN227 4.9 56.3 1.0

S.Steinbacher, J.Kaiser, W.Eisenreich, R.Huber, A.Bacher, F.Rohdich. Structural Basis of Fosmidomycin Action Revealed By the Complex with 2-C-Methyl-D-Erythritol 4-Phosphate Synthase (Ispc). Implications For the Catalytic Mechanism and Anti-Malaria Drug Development. J.Biol.Chem. V. 278 18401 2003.
ISSN: ISSN 0021-9258
PubMed: 12621040
DOI: 10.1074/JBC.M300993200