Manganese in PDB 3i0g: Crystal Structure of Gtb C80S/C196S + Da + Udp-Gal

All present enzymatic activity of Crystal Structure of Gtb C80S/C196S + Da + Udp-Gal:
2.4.1.37;

The structure of Crystal Structure of Gtb C80S/C196S + Da + Udp-Gal, PDB code: 3i0g was solved by B.Schuman, M.Persson, R.C.Landry, R.Polakowski, J.T.Weadge, N.O.L.Seto, S.Borisova, M.M.Palcic, S.V.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.87 / 1.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	52.545, 149.277, 79.454, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 23

The binding sites of Manganese atom in the Crystal Structure of Gtb C80S/C196S + Da + Udp-Gal (pdb code 3i0g). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Gtb C80S/C196S + Da + Udp-Gal, PDB code: 3i0g:

Manganese binding site 1 out of 1 in the Crystal Structure of Gtb C80S/C196S + Da + Udp-Gal


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Gtb C80S/C196S + Da + Udp-Gal within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn2 b:25.4 occ:1.00 OD2 A:ASP211 2.0 18.0 1.0 O A:HOH378 2.2 23.5 1.0 O1A A:UDP358 2.2 19.0 1.0 O A:HOH422 2.2 27.8 1.0 OD2 A:ASP213 2.5 16.2 1.0 O2B A:UDP358 3.0 22.1 1.0 O A:HOH366 3.0 22.1 1.0 OD1 A:ASP213 3.2 29.0 1.0 CG A:ASP211 3.2 15.1 1.0 CG A:ASP213 3.2 16.8 1.0 PB A:UDP358 3.3 25.1 1.0 PA A:UDP358 3.5 19.5 1.0 CB A:ASP211 3.7 12.9 1.0 O3' A:UDP358 3.7 18.0 1.0 O3A A:UDP358 3.9 21.2 1.0 O A:HOH448 4.0 30.2 1.0 O A:HOH528 4.1 36.2 1.0 OD1 A:ASP211 4.1 15.7 1.0 O A:HOH451 4.3 30.4 1.0 C5' A:UDP358 4.3 17.2 1.0 O3B A:UDP358 4.3 25.1 1.0 O5' A:UDP358 4.4 21.1 1.0 C3' A:UDP358 4.5 17.7 1.0 CB A:ASP213 4.6 15.6 1.0 O2A A:UDP358 4.7 21.4 1.0 O1 A:GAL359 4.7 21.5 1.0 O A:HOH450 4.7 30.2 1.0 C4' A:UDP358 4.9 18.3 1.0 CB A:ALA268 4.9 10.9 1.0

B.Schuman, M.Persson, R.C.Landry, R.Polakowski, J.T.Weadge, N.O.Seto, S.N.Borisova, M.M.Palcic, S.V.Evans. Cysteine-to-Serine Mutants Dramatically Reorder the Active Site of Human Abo(H) Blood Group B Glycosyltransferase Without Affecting Activity: Structural Insights Into Cooperative Substrate Binding J.Mol.Biol. V. 402 399 2010.
ISSN: ISSN 0022-2836
PubMed: 20655926
DOI: 10.1016/J.JMB.2010.07.036