Manganese in PDB 4gbp: Crystal Structure of Bbbb+Udp+Gal at pH 10 with Mpd As the Cryoprotectant

All present enzymatic activity of Crystal Structure of Bbbb+Udp+Gal at pH 10 with Mpd As the Cryoprotectant:
2.4.1.37;

The structure of Crystal Structure of Bbbb+Udp+Gal at pH 10 with Mpd As the Cryoprotectant, PDB code: 4gbp was solved by A.R.Johal, J.A.Alfaro, R.J.Blackler, B.Schuman, S.N.Borisova, S.V.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.15
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	52.189, 150.769, 79.397, 90.00, 90.00, 90.00
R / Rfree (%)	16 / 22.5

The binding sites of Manganese atom in the Crystal Structure of Bbbb+Udp+Gal at pH 10 with Mpd As the Cryoprotectant (pdb code 4gbp). 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 Bbbb+Udp+Gal at pH 10 with Mpd As the Cryoprotectant, PDB code: 4gbp:

Manganese binding site 1 out of 1 in the Crystal Structure of Bbbb+Udp+Gal at pH 10 with Mpd As the Cryoprotectant


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 Bbbb+Udp+Gal at pH 10 with Mpd As the Cryoprotectant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:21.6 occ:0.80 O1A A:UDP403 2.1 22.7 0.8 OD2 A:ASP211 2.1 19.2 1.0 O3B A:UDP403 2.2 22.9 0.8 OD1 A:ASP213 2.3 20.9 1.0 OD2 A:ASP213 2.3 24.4 1.0 CG A:ASP213 2.6 23.1 1.0 HB3 A:ASP211 3.1 17.0 1.0 CG A:ASP211 3.2 17.3 1.0 PB A:UDP403 3.2 22.7 0.8 PA A:UDP403 3.4 24.2 0.8 HZ1 A:LYS346 3.4 36.6 1.0 HO2 A:GAL401 3.4 25.2 0.0 O1B A:UDP403 3.6 22.5 0.8 CB A:ASP211 3.6 17.0 1.0 O3A A:UDP403 3.6 22.9 0.8 O3' A:UDP403 3.8 18.0 1.0 HB2 A:ASP211 3.8 16.9 1.0 H5'2 A:UDP403 4.0 23.8 1.0 HZ2 A:LYS346 4.1 36.3 1.0 CB A:ASP213 4.1 20.5 1.0 O2 A:GAL401 4.2 20.0 0.8 NZ A:LYS346 4.2 36.5 1.0 H3 A:GAL401 4.3 20.9 1.0 OD1 A:ASP211 4.3 17.1 1.0 H A:ASP213 4.3 18.2 1.0 C5' A:UDP403 4.3 24.3 1.0 HB1 A:ALA268 4.4 15.6 1.0 O5' A:UDP403 4.4 22.9 0.8 O2A A:UDP403 4.5 22.8 0.8 C3' A:UDP403 4.5 20.0 1.0 HB2 A:ASP213 4.5 20.9 1.0 HB3 A:ASP213 4.5 20.9 1.0 HO3' A:UDP403 4.6 18.3 0.0 O2B A:UDP403 4.6 20.8 0.8 H3' A:UDP403 4.6 21.1 1.0 HE1 A:TYR126 4.7 29.3 1.0 HE3 A:LYS346 4.8 36.7 1.0 HG2 A:MET214 4.8 20.9 1.0 C4' A:UDP403 4.8 21.7 1.0 O A:HOH528 4.8 30.1 1.0 HZ3 A:LYS346 4.8 36.6 1.0 H4' A:UDP403 4.9 22.3 1.0 H1 A:GAL401 5.0 20.3 1.0 SD A:MET214 5.0 23.5 1.0 HB2 A:ALA268 5.0 15.5 1.0 CA A:ASP211 5.0 16.3 1.0

A.R.Johal, R.J.Blackler, J.A.Alfaro, B.Schuman, S.Borisova, S.V.Evans. pH-Induced Conformational Changes in Human Abo(H) Blood Group Glycosyltransferases Confirm the Importance of Electrostatic Interactions in the Formation of the Semi-Closed State. Glycobiology V. 24 237 2014.
ISSN: ISSN 0959-6658
PubMed: 24265507
DOI: 10.1093/GLYCOB/CWT098