Manganese in PDB 5c4d: Crystal Structure of Gtb + Udp-Glc + Di

All present enzymatic activity of Crystal Structure of Gtb + Udp-Glc + Di:
2.4.1.37; 2.4.1.40;

The structure of Crystal Structure of Gtb + Udp-Glc + Di, PDB code: 5c4d was solved by S.Gagnon, P.Meloncelli, R.B.Zheng, O.Haji-Ghassemi, A.R.Johal, S.Borisova, T.L.Lowary, S.V.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.79 / 1.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	52.640, 149.580, 79.230, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 18.9

The binding sites of Manganese atom in the Crystal Structure of Gtb + Udp-Glc + Di (pdb code 5c4d). 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 + Udp-Glc + Di, PDB code: 5c4d:

Manganese binding site 1 out of 1 in the Crystal Structure of Gtb + Udp-Glc + Di


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 + Udp-Glc + Di within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:23.4 occ:1.00 O A:HOH719 2.2 25.8 1.0 O1A A:UPG403 2.2 14.4 1.0 OD1 A:ASP213 2.2 13.6 1.0 O2B A:UPG403 2.3 22.5 1.0 OD2 A:ASP213 2.7 20.7 1.0 OD2 A:ASP211 2.7 17.5 1.0 CG A:ASP213 2.8 15.8 1.0 O A:HOH567 3.0 39.5 1.0 PB A:UPG403 3.4 20.0 1.0 PA A:UPG403 3.5 15.5 1.0 O3B A:UPG403 3.6 18.8 1.0 CG A:ASP211 3.7 14.3 1.0 O3A A:UPG403 3.7 16.4 1.0 O A:HOH646 3.7 29.4 1.0 CB A:ASP211 3.8 13.3 1.0 O3C A:UPG403 3.9 14.3 1.0 O A:HOH522 4.2 27.0 1.0 NZ A:LYS346 4.3 38.4 1.0 CB A:ASP213 4.3 14.1 1.0 C5C A:UPG403 4.4 14.1 1.0 O5C A:UPG403 4.5 14.4 1.0 CE A:LYS346 4.5 40.2 1.0 O2A A:UPG403 4.5 16.0 1.0 O A:HOH506 4.6 23.6 1.0 C3C A:UPG403 4.7 14.0 1.0 O1B A:UPG403 4.8 22.6 1.0 OD1 A:ASP211 4.8 15.3 1.0 O A:ASP213 4.9 13.1 1.0

S.M.Gagnon, P.J.Meloncelli, R.B.Zheng, O.Haji-Ghassemi, A.R.Johal, S.N.Borisova, T.L.Lowary, S.V.Evans. High Resolution Structures of the Human Abo(H) Blood Group Enzymes in Complex with Donor Analogs Reveal That the Enzymes Utilize Multiple Donor Conformations to Bind Substrates in A Stepwise Manner. J.Biol.Chem. V. 290 27040 2015.
ISSN: ESSN 1083-351X
PubMed: 26374898
DOI: 10.1074/JBC.M115.682401