Manganese in PDB 4mu1: The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+, Imidazole, and Sulfate at 1.5 A Resoltuion

All present enzymatic activity of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+, Imidazole, and Sulfate at 1.5 A Resoltuion:
4.2.1.19;

The structure of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+, Imidazole, and Sulfate at 1.5 A Resoltuion, PDB code: 4mu1 was solved by C.Bisson, K.L.Britton, S.E.Sedelnikova, P.J.Baker, D.W.Rice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.26 / 1.50
Space group	P 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	113.880, 113.880, 113.880, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 18.8

The binding sites of Manganese atom in the The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+, Imidazole, and Sulfate at 1.5 A Resoltuion (pdb code 4mu1). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+, Imidazole, and Sulfate at 1.5 A Resoltuion, PDB code: 4mu1:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+, Imidazole, and Sulfate at 1.5 A Resoltuion


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+, Imidazole, and Sulfate at 1.5 A Resoltuion within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:17.0 occ:1.00 NE2 A:HIS74 2.3 20.4 1.0 O A:HOH404 2.3 24.3 1.0 CE1 A:HIS74 3.0 18.5 1.0 CD2 A:HIS74 3.5 26.3 1.0 N1 A:IMD303 3.5 19.2 1.0 C2 A:IMD303 3.9 19.8 1.0 ND1 A:HIS74 4.3 24.1 1.0 CG A:HIS74 4.5 22.9 1.0 C5 A:IMD303 4.7 19.8 1.0

Manganese binding site 2 out of 2 in the The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+, Imidazole, and Sulfate at 1.5 A Resoltuion


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+, Imidazole, and Sulfate at 1.5 A Resoltuion within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:11.6 occ:1.00 O A:HOH401 2.2 13.6 1.0 N3 A:IMD303 2.2 19.0 1.0 NE2 A:HIS73 2.2 12.6 1.0 OE1 A:GLU77 2.3 12.2 1.0 NE2 A:HIS145 2.3 11.2 1.0 C4 A:IMD303 3.2 20.4 1.0 CE1 A:HIS73 3.2 12.3 1.0 C2 A:IMD303 3.2 19.8 1.0 CE1 A:HIS145 3.2 12.9 1.0 CD A:GLU77 3.2 11.4 1.0 CD2 A:HIS73 3.3 13.5 1.0 CD2 A:HIS145 3.3 12.3 1.0 OE2 A:GLU77 3.6 11.9 1.0 ND1 A:HIS73 4.3 12.0 1.0 C5 A:IMD303 4.3 19.8 1.0 N1 A:IMD303 4.3 19.2 1.0 ND1 A:HIS145 4.4 12.0 1.0 CG A:HIS73 4.4 11.1 1.0 CG A:HIS145 4.4 11.1 1.0 CG A:GLU77 4.5 11.4 1.0 CB A:GLU77 4.8 12.6 1.0 O A:HOH414 4.9 12.5 1.0

C.Bisson, K.L.Britton, S.E.Sedelnikova, H.F.Rodgers, T.C.Eadsforth, R.Viner, T.R.Hawkes, P.J.Baker, D.W.Rice. A New Role For Metal Ions in Enzyme Catalysis To Be Published.