Manganese in PDB 4qnj: The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution

All present enzymatic activity of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution:
4.2.1.19;

The structure of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution, PDB code: 4qnj was solved by 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, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.91 / 1.30
Space group	P 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	114.150, 114.150, 114.150, 90.00, 90.00, 90.00
R / Rfree (%)	13.3 / 14.4

The structure of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution (pdb code 4qnj). 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+ and Formate at 1.3A Resolution, PDB code: 4qnj:
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+ and Formate at 1.3A Resolution


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+ and Formate at 1.3A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:8.7 occ:1.00 O A:HOH598 2.2 9.9 1.0 O2 A:FMT303 2.2 11.0 1.0 NE2 A:HIS73 2.3 9.5 1.0 OE1 A:GLU77 2.3 9.6 1.0 NE2 A:HIS145 2.3 9.1 1.0 CD A:GLU77 3.2 8.8 1.0 CE1 A:HIS73 3.2 9.1 1.0 C A:FMT303 3.2 12.8 1.0 CD2 A:HIS73 3.3 8.9 1.0 CD2 A:HIS145 3.3 8.4 1.0 CE1 A:HIS145 3.3 8.9 1.0 OE2 A:GLU77 3.6 9.2 1.0 O A:HOH538 4.0 23.4 1.0 O1 A:FMT303 4.3 11.7 1.0 ND1 A:HIS73 4.3 9.2 1.0 ND1 A:HIS145 4.4 8.3 1.0 CG A:HIS73 4.4 8.6 1.0 CG A:HIS145 4.4 7.6 1.0 CG A:GLU77 4.5 9.2 1.0 CB A:GLU77 4.7 8.4 1.0 O A:HOH405 4.9 9.9 1.0 O A:HOH602 5.0 34.5 1.0

Manganese binding site 2 out of 2 in the The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution


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+ and Formate at 1.3A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:10.2 occ:1.00 O1 A:FMT303 2.2 11.7 1.0 NE2 A:HIS74 2.3 9.8 1.0 O A:HOH401 2.3 12.1 1.0 C A:FMT303 3.2 12.8 1.0 CE1 A:HIS74 3.2 10.3 1.0 CD2 A:HIS74 3.3 10.3 1.0 O A:HOH504 4.1 32.3 1.0 ND1 A:HIS74 4.3 10.8 1.0 O2 A:FMT303 4.4 11.0 1.0 CG A:HIS74 4.4 9.9 1.0

C.Bisson, K.L.Britton, S.E.Sedelnikova, H.F.Rodgers, T.C.Eadsforth, R.C.Viner, T.R.Hawkes, P.J.Baker, D.W.Rice. Crystal Structures Reveal That the Reaction Mechanism of Imidazoleglycerol-Phosphate Dehydratase Is Controlled By Switching Mn(II) Coordination. Structure V. 23 1236 2015.
ISSN: ISSN 0969-2126
PubMed: 26095028
DOI: 10.1016/J.STR.2015.05.012