Manganese in PDB 1ono: Ispc MN2+ Complex

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

The structure of Ispc MN2+ Complex, PDB code: 1ono 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 (°)	91.388, 52.249, 108.327, 90.00, 92.52, 90.00
R / Rfree (%)	21.6 / 28.7

The binding sites of Manganese atom in the Ispc MN2+ Complex (pdb code 1ono). 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 MN2+ Complex, PDB code: 1ono:
Jump to Manganese binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Ispc MN2+ Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1001 b:49.6 occ:1.00 O A:HOH1096 2.2 50.8 1.0 O A:HOH1097 2.2 59.6 1.0 O A:HOH1095 2.2 45.0 1.0 OE1 A:GLU231 2.4 44.9 1.0 OE2 A:GLU152 2.4 51.1 1.0 OD1 A:ASP150 2.5 41.9 1.0 CG A:ASP150 3.2 53.8 1.0 OD2 A:ASP150 3.2 53.0 1.0 CD A:GLU152 3.4 46.3 1.0 CD A:GLU231 3.5 47.4 1.0 OE1 A:GLU152 3.7 52.7 1.0 OE2 A:GLU231 4.2 47.2 1.0 NZ A:LYS125 4.2 65.3 1.0 N A:SER151 4.5 47.5 1.0 N A:GLU152 4.5 38.4 1.0 ND2 A:ASN227 4.6 57.4 1.0 CB A:SER151 4.6 41.7 1.0 CB A:ASP150 4.6 49.7 1.0 CG A:GLU152 4.6 44.5 1.0 OD1 A:ASN227 4.7 59.4 1.0 CG A:GLU231 4.7 45.4 1.0 CB A:GLU152 4.8 40.6 1.0

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Ispc MN2+ Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1001 b:49.5 occ:1.00 O B:HOH1107 2.2 46.1 1.0 O B:HOH1106 2.2 48.2 1.0 O B:HOH1108 2.2 56.7 1.0 OE2 B:GLU152 2.3 53.2 1.0 OE1 B:GLU231 2.4 43.4 1.0 OD1 B:ASP150 2.4 42.5 1.0 CG B:ASP150 3.2 53.8 1.0 OD2 B:ASP150 3.2 57.9 1.0 CD B:GLU152 3.3 50.4 1.0 CD B:GLU231 3.6 43.8 1.0 OE1 B:GLU152 3.6 53.0 1.0 OE2 B:GLU231 4.2 45.8 1.0 NZ B:LYS125 4.3 61.3 1.0 N B:SER151 4.6 47.8 1.0 N B:GLU152 4.6 41.9 1.0 CB B:SER151 4.6 40.9 1.0 ND2 B:ASN227 4.6 60.5 1.0 CB B:ASP150 4.6 48.2 1.0 CG B:GLU152 4.6 47.8 1.0 OD1 B:ASN227 4.7 60.4 1.0 CG B:GLU231 4.8 44.4 1.0 O B:HOH1037 4.9 44.3 1.0 CB B:GLU152 4.9 44.8 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