Manganese in PDB 2rix: B-Specific-1,3-Galactosyltransferase)(Gtb) + Udp

All present enzymatic activity of B-Specific-1,3-Galactosyltransferase)(Gtb) + Udp:
2.4.1.37;

The structure of B-Specific-1,3-Galactosyltransferase)(Gtb) + Udp, PDB code: 2rix was solved by S.V.Evans, J.A.Alfaro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.83 / 1.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	52.540, 149.930, 79.280, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 23.1

The binding sites of Manganese atom in the B-Specific-1,3-Galactosyltransferase)(Gtb) + Udp (pdb code 2rix). 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 B-Specific-1,3-Galactosyltransferase)(Gtb) + Udp, PDB code: 2rix:

Manganese binding site 1 out of 1 in the B-Specific-1,3-Galactosyltransferase)(Gtb) + Udp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of B-Specific-1,3-Galactosyltransferase)(Gtb) + Udp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1 b:34.4 occ:1.00 O1A A:UDP356 2.2 21.2 0.5 OD2 A:ASP211 2.3 21.8 1.0 O2B A:UDP356 2.3 30.5 0.5 OD1 A:ASP213 2.5 18.7 1.0 OD2 A:ASP213 2.9 26.6 1.0 CG A:ASP213 3.1 18.6 1.0 PB A:UDP356 3.1 33.0 0.5 O3B A:UDP356 3.1 38.3 1.0 CG A:ASP211 3.2 16.7 1.0 PA A:UDP356 3.4 26.7 0.5 CB A:ASP211 3.5 16.2 1.0 O3A A:UDP356 3.6 30.2 0.5 O3' A:UDP356 3.8 28.5 1.0 O5' A:UDP356 3.9 28.7 0.5 OD1 A:ASP211 4.3 18.6 1.0 C3' A:UDP356 4.5 28.5 1.0 O1B A:UDP356 4.6 31.9 0.5 CB A:ASP213 4.6 17.9 1.0 O2A A:UDP356 4.6 27.2 0.5 C4' A:UDP356 4.7 29.9 1.0 C5' A:UDP356 4.9 30.2 1.0 CB A:ALA268 4.9 16.1 1.0 CA A:ASP211 5.0 15.8 1.0 O A:ASP213 5.0 16.2 1.0

J.A.Alfaro, R.B.Zheng, M.Persson, J.A.Letts, R.Polakowski, Y.Bai, S.N.Borisova, N.O.Seto, T.L.Lowary, M.M.Palcic, S.V.Evans. Abo(H) Blood Group A and B Glycosyltransferases Recognize Substrate Via Specific Conformational Changes. J.Biol.Chem. V. 283 10097 2008.
ISSN: ISSN 0021-9258
PubMed: 18192272
DOI: 10.1074/JBC.M708669200