Manganese in PDB 8ui6: X-Ray Crystal Structure of Toxoplasma Gondii Galnac-T3 in Complex with Udp-Galnac, MN2+, and MUC5AC-3,13

All present enzymatic activity of X-Ray Crystal Structure of Toxoplasma Gondii Galnac-T3 in Complex with Udp-Galnac, MN2+, and MUC5AC-3,13:
2.4.1.41;

The structure of X-Ray Crystal Structure of Toxoplasma Gondii Galnac-T3 in Complex with Udp-Galnac, MN2+, and MUC5AC-3,13, PDB code: 8ui6 was solved by P.Kumar, N.L.Samara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 2.65
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.252, 66.913, 163.581, 90, 90, 90
R / Rfree (%)	17.5 / 23.2

The binding sites of Manganese atom in the X-Ray Crystal Structure of Toxoplasma Gondii Galnac-T3 in Complex with Udp-Galnac, MN2+, and MUC5AC-3,13 (pdb code 8ui6). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the X-Ray Crystal Structure of Toxoplasma Gondii Galnac-T3 in Complex with Udp-Galnac, MN2+, and MUC5AC-3,13, PDB code: 8ui6:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the X-Ray Crystal Structure of Toxoplasma Gondii Galnac-T3 in Complex with Udp-Galnac, MN2+, and MUC5AC-3,13


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of X-Ray Crystal Structure of Toxoplasma Gondii Galnac-T3 in Complex with Udp-Galnac, MN2+, and MUC5AC-3,13 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn701 b:41.4 occ:1.00 O1A A:UDP702 2.1 53.5 1.0 OD2 A:ASP276 2.2 58.3 1.0 O A:HOH813 2.2 41.5 1.0 O1B A:UDP702 2.2 47.6 1.0 NE2 A:HIS414 2.3 38.3 1.0 NE2 A:HIS278 2.3 37.0 1.0 CE1 A:HIS414 3.0 35.1 1.0 HE1 A:HIS414 3.0 42.0 1.0 CE1 A:HIS278 3.1 46.0 1.0 HE1 A:HIS278 3.1 55.1 1.0 PA A:UDP702 3.3 47.3 1.0 PB A:UDP702 3.3 55.1 1.0 CG A:ASP276 3.3 56.1 1.0 H5'2 A:UDP702 3.4 66.7 1.0 O3A A:UDP702 3.4 62.2 1.0 CD2 A:HIS278 3.4 37.8 1.0 CD2 A:HIS414 3.4 39.3 1.0 O2B A:UDP702 3.6 82.7 1.0 HB3 A:ASP276 3.6 64.4 1.0 HD2 A:HIS278 3.7 45.2 1.0 HD2 A:HIS414 3.7 47.0 1.0 CB A:ASP276 4.0 53.7 1.0 H3' A:UDP702 4.0 67.4 1.0 ND1 A:HIS414 4.2 42.6 1.0 C5' A:UDP702 4.2 55.6 1.0 HH11 A:ARG417 4.2 69.2 1.0 O5' A:UDP702 4.2 61.4 1.0 HB2 A:ASP276 4.3 64.4 1.0 OD1 A:ASP276 4.3 67.0 1.0 HH12 A:ARG417 4.3 69.2 1.0 ND1 A:HIS278 4.3 35.5 1.0 O2A A:UDP702 4.3 57.0 1.0 O A:ILE415 4.4 55.6 1.0 CG A:HIS414 4.4 40.5 1.0 CG A:HIS278 4.5 45.6 1.0 NH1 A:ARG417 4.5 57.8 1.0 O3B A:UDP702 4.6 65.9 1.0 O A:HOH814 4.7 51.4 1.0 C3' A:UDP702 4.8 56.2 1.0 H5'1 A:UDP702 4.9 66.7 1.0 HG3 A:ARG417 4.9 85.6 1.0 HD1 A:HIS414 4.9 51.0 1.0

Manganese binding site 2 out of 2 in the X-Ray Crystal Structure of Toxoplasma Gondii Galnac-T3 in Complex with Udp-Galnac, MN2+, and MUC5AC-3,13


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of X-Ray Crystal Structure of Toxoplasma Gondii Galnac-T3 in Complex with Udp-Galnac, MN2+, and MUC5AC-3,13 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn703 b:64.0 occ:0.51 OE2 A:GLU336 2.2 79.8 1.0 O A:HOH809 2.2 53.3 1.0 O A:HOH818 2.2 64.2 1.0 O A:HOH816 2.2 65.9 1.0 NE2 A:HIS333 2.3 63.9 1.0 CD A:GLU336 2.3 78.4 1.0 OE1 A:GLU336 2.4 82.2 1.0 HE1 A:HIS333 3.0 52.1 1.0 CE1 A:HIS333 3.0 43.5 1.0 CG A:GLU336 3.4 57.0 1.0 HG2 A:GLU336 3.4 68.3 1.0 CD2 A:HIS333 3.4 42.4 1.0 HG3 A:GLU336 3.6 68.3 1.0 HD2 A:HIS333 3.7 50.8 1.0 ND1 A:HIS333 4.2 40.9 1.0 O A:CYS566 4.2 67.5 1.0 HH12 A:ARG567 4.3 116.9 1.0 HD22 A:LEU327 4.4 49.5 1.0 CG A:HIS333 4.4 37.9 1.0 NH1 A:ARG567 4.4 97.5 1.0 HH11 A:ARG567 4.5 116.9 1.0 CB A:GLU336 4.7 56.2 1.0 HB3 A:GLU336 4.8 67.4 1.0 OE1 A:GLU554 4.8 47.8 1.0 HD1 A:HIS333 4.9 49.0 1.0 HG2 A:GLU554 4.9 63.5 1.0 CZ A:ARG567 4.9 92.7 1.0 HD3 A:ARG567 4.9 98.6 1.0 HB2 A:CYS566 4.9 70.2 1.0 HE1 A:HIS338 5.0 68.6 1.0

P.Kumar, T.Tomita, T.A.Gerken, C.J.Ballard, Y.S.Lee, L.M.Weiss, N.L.Samara. A Toxoplasma Gondii O-Glycosyltransferase That Modulates Bradyzoite Cyst Wall Rigidity Is Distinct From Host Homologues Nat Commun V. 15 3792 2024.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-024-48253-W